Gordon G. Hammes | Scholars@Duke

Gordon G. Hammes
University Distinguished Service Professor Emeritus of Biochemistry

My research is concerned with studying the dynamics of single enzyme molecules with fluorescence microscopy. The principle of the method used is to fix the active enzyme to the surface of a slide and to view the trajectory (time course) of the enzyme during the course of ligand binding and/or catalysis. The enzyme is labeled with a fluorescent tag that monitors events on the enzyme through changes in fluorescence. Methods are being developed for both the fluorescent labeling of the enzymes and their attachment to the quartz slide. Single molecule kinetics have the potential of revealing steps in the catalytic process that cannot be observed with ensemble averaged kinetics. These include direct observation of the coupling of the enzyme conformation to catalysis, monitoring the conformation of different parts of a single enzyme molecule simultaneously, and dissection of processive reactions, such as DNA synthesis, into the individual steps in the reaction. Two enzymes are being investigated, dihydrofolate reductase (DHFR) and T4 DNA polymerase. The trajectories of individual DHFR molecules reacting with substrates and methotrexate reveal conformational changes that are not seen with ensemble averaged kinetics. An isotope rate effect for the hydride transfer has been observed at the single molecule level. In the case of T4 DNA polymerase, experiments are being carried out in which the DNA template is attached to the slide. Assembly of the protein complex necessary for catalysis and the enzymatic reaction are being studied. Thse experiments are directed at understanding better how enzymes catalyze physiological reactions.

Current Appointments & Affiliations

University Distinguished Service Professor Emeritus of Biochemistry, Biochemistry, Basic Science Departments 2008
Professor Emeritus of Biochemistry, Biochemistry, Basic Science Departments 2008

Contact Information

436A Nanaline H Duke, Durham, NC 27710
Box 3711 Med Ctr, Durham, NC 27710
hamme001@mc.duke.edu (919) 684-5519

Background
Education, Training, & Certifications
- Ph.D., University of Wisconsin, Madison 1959
Duke Appointment History
- Professor of Biochemistry, Biochemistry, Basic Science Departments 1992 - 2007
- Vice Chancellor for Medical Center Academic Affairs, School of Medicine, Duke University 1991 - 1998
Research
Selected Grants
- Single Molecule Studies of Enzyme Catalysis awarded by National Institutes of Health 2002 - 2007
- Zeiss LSM510 META confocal-fluorescence spectroscopy awarded by National Institutes of Health 2003 - 2004
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Hammes, Gordon G., Yu-Chu Chang, and Terrence G. Oas. “Conformational selection or induced fit: a flux description of reaction mechanism.” Proc Natl Acad Sci U S A 106, no. 33 (August 18, 2009): 13737–41. https://doi.org/10.1073/pnas.0907195106.
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  - Hammes, Gordon G. “How do enzymes really work?” J Biol Chem 283, no. 33 (August 15, 2008): 22337–46. https://doi.org/10.1074/jbc.X800005200.
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  - Zhang, Zhiquan, PT Ravi Rajagopalan, Tzvia Selzer, Stephen J. Benkovic, and Gordon G. Hammes. “Single-molecule and transient kinetics investigation of the interaction of dihydrofolate reductase with NADPH and dihydrofolate.” Proc Natl Acad Sci U S A 101, no. 9 (March 2, 2004): 2764–69. https://doi.org/10.1073/pnas.0400091101.
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  - Hammes, Gordon G. “Walter Kauzmann: an undergraduate perspective.” Biophys Chem 105, no. 2–3 (September 2003): 167. https://doi.org/10.1016/s0301-4622(03)00080-2.
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  - Rajagopalan, PT Ravi, Zhiquan Zhang, Lynn McCourt, Mary Dwyer, Stephen J. Benkovic, and Gordon G. Hammes. “Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics.” Proc Natl Acad Sci U S A 99, no. 21 (October 15, 2002): 13481–86. https://doi.org/10.1073/pnas.172501499.
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  - Hammes, Gordon G. “Multiple conformational changes in enzyme catalysis.” Biochemistry 41, no. 26 (July 2, 2002): 8221–28. https://doi.org/10.1021/bi0260839.
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  - Tillman, P Glynn, Glenn G. Hammes, Matthew Sacher, Michael Connair, E Angela Brady, and Keith D. Wing. “Toxicity of a formulation of the insecticide indoxacarb to the tarnished plant bug, Lygus lineolaris (Hemiptera: Miridae), and the big-eyed bug, Geocoris punctipes (Hemiptera: Lygaeidae).” Pest Manag Sci 58, no. 1 (January 2002): 92–100. https://doi.org/10.1002/ps.426.
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  - Hammes, G. G. “Editorial.” Biochemistry 38, no. 1 (January 5, 1999): 1. https://doi.org/10.1021/bi9900018.
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  - Hammes, G. G. “A golden era for understanding enzyme mechanisms.” Protein Sci 7, no. 3 (March 1998): 799–802. https://doi.org/10.1002/pro.5560070331.
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  - Fierke, C. A., and G. G. Hammes. “Transient kinetic approaches to enzyme mechanisms.” Methods Enzymol 249 (1995): 3–37. https://doi.org/10.1016/0076-6879(95)49029-9.
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  - Mitra, B., and G. G. Hammes. “Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles.” Biochemistry 29, no. 42 (October 23, 1990): 9879–84. https://doi.org/10.1021/bi00494a018.
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  - Musier-Forsyth, K. M., and G. G. Hammes. “Rotational dynamics of chloroplast ATP synthase in phospholipid vesicles.” Biochemistry 29, no. 13 (April 3, 1990): 3236–41. https://doi.org/10.1021/bi00465a014.
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  - Davis, C. B., K. E. Smith, B. N. Campbell, and G. G. Hammes. “The ATP binding site of the yeast plasma membrane proton-translocating ATPase.” J Biol Chem 265, no. 3 (January 25, 1990): 1300–1305.
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  - Chang, S. I., and G. G. Hammes. “Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast.” Proc Natl Acad Sci U S A 86, no. 21 (November 1989): 8373–76. https://doi.org/10.1073/pnas.86.21.8373.
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  - Holzer, K. P., and G. G. Hammes. “Cloning and expression of the yeast plasma membrane ATPase in Escherichia coli.” J Biol Chem 264, no. 24 (August 25, 1989): 14389–95.
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  - Holzer, K. P., W. Liu, and G. G. Hammes. “Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA.” Proc Natl Acad Sci U S A 86, no. 12 (June 1989): 4387–91. https://doi.org/10.1073/pnas.86.12.4387.
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  - Chang, S. I., and G. G. Hammes. “Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase.” Biochemistry 28, no. 9 (May 2, 1989): 3781–88. https://doi.org/10.1021/bi00435a023.
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  - Mitra, B., and G. G. Hammes. “Structural map of the dicyclohexylcarbodiimide site of chloroplast coupling factor determined by resonance energy transfer.” Biochemistry 28, no. 7 (April 4, 1989): 3063–69. https://doi.org/10.1021/bi00433a049.
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  - Davis, C. B., and G. G. Hammes. “Topology of the yeast plasma membrane proton-translocating ATPase.” J Biol Chem 264, no. 1 (January 5, 1989): 370–74.
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  - Smith, K. E., and G. G. Hammes. “Studies of the phosphoenzyme intermediate of the yeast plasma membrane proton-translocating ATPase.” J Biol Chem 263, no. 27 (September 25, 1988): 13774–78.
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  - Musier, K. M., and G. G. Hammes. “Assessment of the number of nucleotide binding sites on chloroplast coupling factor 1 by the continuous variation method.” Biochemistry 27, no. 18 (September 6, 1988): 7015–20. https://doi.org/10.1021/bi00418a052.
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  - Yuan, Z. Y., W. Liu, and G. G. Hammes. “Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase mRNA.” Proc Natl Acad Sci U S A 85, no. 17 (September 1988): 6328–31. https://doi.org/10.1073/pnas.85.17.6328.
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  - Kashem, M. A., and G. G. Hammes. “Correlation of enzymatic activities and aggregation state in chicken liver fatty acid synthase.” Biochim Biophys Acta 956, no. 1 (August 31, 1988): 39–48. https://doi.org/10.1016/0167-4838(88)90295-6.
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  - Chang, S. I., and G. G. Hammes. “Amino acid sequences of substrate-binding sites in chicken liver fatty acid synthase.” Biochemistry 27, no. 13 (June 28, 1988): 4753–60. https://doi.org/10.1021/bi00413a026.
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  - Leckband, D., and G. G. Hammes. “Function of tightly bound nucleotides on membrane-bound chloroplast coupling factor.” Biochemistry 27, no. 10 (May 17, 1988): 3629–33. https://doi.org/10.1021/bi00410a016.
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  - Mitra, B., and G. G. Hammes. “Characterization of three-subunit chloroplast coupling factor.” Biochemistry 27, no. 1 (January 12, 1988): 245–50. https://doi.org/10.1021/bi00401a037.
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  - Musier, K. M., and G. G. Hammes. “Rotation of nucleotide sites is not required for the enzymatic activity of chloroplast coupling factor 1.” Biochemistry 26, no. 19 (September 22, 1987): 5982–88. https://doi.org/10.1021/bi00393a006.
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  - Admon, A., and G. G. Hammes. “Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1.” Biochemistry 26, no. 11 (June 2, 1987): 3193–97. https://doi.org/10.1021/bi00385a038.
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  - Leckband, D., and G. G. Hammes. “Interactions between nucleotide binding sites on chloroplast coupling factor during ATP hydrolysis.” Biochemistry 26, no. 8 (April 21, 1987): 2306–12. https://doi.org/10.1021/bi00382a035.
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  - Yuan, Z. Y., and G. G. Hammes. “Fluorescence studies of chicken liver fatty acid synthase. Segmental flexibility and distance measurements.” J Biol Chem 261, no. 29 (October 15, 1986): 13643–51.
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  - Leanz, G. F., and G. G. Hammes. “Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.” Biochemistry 25, no. 19 (September 23, 1986): 5617–24. https://doi.org/10.1021/bi00367a041.
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  - Chang, S. I., and G. G. Hammes. “Interaction of spin-labeled nicotinamide adenine dinucleotide phosphate with chicken liver fatty acid synthase.” Biochemistry 25, no. 16 (August 12, 1986): 4661–68. https://doi.org/10.1021/bi00364a031.
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  - Schinkel, J. E., and G. G. Hammes. “Chloroplast coupling factor 1: dependence of rotational correlation time on polypeptide composition.” Biochemistry 25, no. 14 (July 15, 1986): 4066–71. https://doi.org/10.1021/bi00362a012.
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  - Krupinski, J., and G. G. Hammes. “Steady-state ATP synthesis by bacteriorhodopsin and chloroplast coupling factor co-reconstituted into asolectin vesicles.” Proc Natl Acad Sci U S A 83, no. 12 (June 1986): 4233–37. https://doi.org/10.1073/pnas.83.12.4233.
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  - Koland, J. G., and G. G. Hammes. “Steady state kinetic studies of purified yeast plasma membrane proton-translocating ATPase.” J Biol Chem 261, no. 13 (May 5, 1986): 5936–42.
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  - Krupinski, J., and G. G. Hammes. “Phase-lifetime spectrophotometry of deoxycholate-purified bacteriorhodopsin reconstituted into asolectin vesicles.” Biochemistry 24, no. 24 (November 19, 1985): 6963–72. https://doi.org/10.1021/bi00345a032.
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  - Yuan, Z. Y., and G. G. Hammes. “Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. Acylation of specific binding sites.” J Biol Chem 260, no. 25 (November 5, 1985): 13532–38.
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  - Richter, M. L., B. Snyder, R. E. McCarty, and G. G. Hammes. “Binding stoichiometry and structural mapping of the epsilon polypeptide of chloroplast coupling factor 1.” Biochemistry 24, no. 21 (October 8, 1985): 5755–63. https://doi.org/10.1021/bi00342a011.
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  - Anderson, V. E., and G. G. Hammes. “Distribution of reaction intermediates on chicken liver fatty acid synthase.” Biochemistry 24, no. 9 (April 23, 1985): 2147–54. https://doi.org/10.1021/bi00330a007.
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  - Snyder, B., and G. G. Hammes. “Structural organization of chloroplast coupling factor.” Biochemistry 24, no. 9 (April 23, 1985): 2324–31. https://doi.org/10.1021/bi00330a030.
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  - Kambouris, N. G., and G. G. Hammes. “Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.” Proc Natl Acad Sci U S A 82, no. 7 (April 1985): 1950–53. https://doi.org/10.1073/pnas.82.7.1950.
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  - Cognet, J. A., and G. G. Hammes. “Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: beta-ketoacyl reductase and enoyl reductase.” Biochemistry 24, no. 2 (January 15, 1985): 290–97. https://doi.org/10.1021/bi00323a008.
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  - Hammes, G. G. “Fatty acid synthase: elementary steps in catalysis and regulation.” Curr Top Cell Regul 26 (1985): 311–24. https://doi.org/10.1016/b978-0-12-152826-3.50030-9.
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  - Snyder, B., and G. G. Hammes. “Structural mapping of chloroplast coupling factor.” Biochemistry 23, no. 24 (November 20, 1984): 5787–95. https://doi.org/10.1021/bi00319a018.
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  - Waskiewicz, D. E., and G. G. Hammes. “Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation.” Biochemistry 23, no. 14 (July 3, 1984): 3136–43. https://doi.org/10.1021/bi00309a005.
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  - Yuan, Z., and G. G. Hammes. “Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. pH dependence of NADPH binding and isotope rate effect for beta-ketoacyl reductase.” J Biol Chem 259, no. 11 (June 10, 1984): 6748–51.
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  - Anderson, V. E., and G. G. Hammes. “Stereochemistry of the reactions catalyzed by chicken liver fatty acid synthase.” Biochemistry 23, no. 9 (April 24, 1984): 2088–94. https://doi.org/10.1021/bi00304a033.
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  - Cognet, J. A., B. G. Cox, and G. G. Hammes. “Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: reduced nicotinamide adenine dinucleotide phosphate binding and formation and reduction of acetoacetyl-enzyme.” Biochemistry 22, no. 26 (December 20, 1983): 6281–87. https://doi.org/10.1021/bi00295a037.
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  - Krupinski, J., J. L. Spudich, and G. G. Hammes. “Phase-lifetime spectrophotometry of membranes from ion flux mutants of Halobacterium halobium.” J Biol Chem 258, no. 13 (July 10, 1983): 7964–67.
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  - Cox, B. G., and G. G. Hammes. “Steady-state kinetic study of fatty acid synthase from chicken liver.” Proc Natl Acad Sci U S A 80, no. 14 (July 1983): 4233–37. https://doi.org/10.1073/pnas.80.14.4233.
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  - Anderson, V. E., and G. G. Hammes. “Fluorescent properties of pyrene bound at specific acylation sites of chicken liver fatty acid synthase.” Biochemistry 22, no. 12 (June 7, 1983): 2995–3001. https://doi.org/10.1021/bi00281a032.
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  - Cognet, J. A., and G. G. Hammes. “Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: acetylation-deacetylation.” Biochemistry 22, no. 12 (June 7, 1983): 3002–7. https://doi.org/10.1021/bi00281a033.
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  - Cardon, J. W., and G. G. Hammes. “Kinetic and structural investigation of acyl-binding sites on avian fatty acid synthase.” J Biol Chem 258, no. 8 (April 25, 1983): 4802–7.
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  - Cerione, R. A., R. E. McCarty, and G. G. Hammes. “Spatial relationships between specific sites on reconstituted chloroplast proton adenosinetriphosphatase and the phospholipid vesicle surface.” Biochemistry 22, no. 4 (February 15, 1983): 769–76. https://doi.org/10.1021/bi00273a010.
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  - Waskiewicz, D. E., and G. G. Hammes. “Fluorescence polarization study of the alpha-ketoglutarate dehydrogenase complex from Escherichia coli.” Biochemistry 21, no. 25 (December 7, 1982): 6489–96. https://doi.org/10.1021/bi00268a026.
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  - Hammes, G. G. “Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.” Proc Natl Acad Sci U S A 79, no. 22 (November 1982): 6881–84. https://doi.org/10.1073/pnas.79.22.6881.
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  - Bruist, M. F., and G. G. Hammes. “Mechanism for catalysis and regulation of adenosine 5'-triphosphate hydrolysis by chloroplast coupling factor 1.” Biochemistry 21, no. 14 (July 6, 1982): 3370–77. https://doi.org/10.1021/bi00257a019.
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  - Cardon, J. W., and G. G. Hammes. “Investigation of reduced nicotinamide adenine dinucleotide phosphate and acyl-binding sites on avian fatty acid synthase.” Biochemistry 21, no. 12 (June 8, 1982): 2863–70. https://doi.org/10.1021/bi00541a009.
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  - Cerione, R. A., and G. G. Hammes. “Structural mapping of nucleotide binding sites on chloroplast coupling factor.” Biochemistry 21, no. 4 (February 16, 1982): 745–52. https://doi.org/10.1021/bi00533a026.
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  - Dewey, T. G., and G. G. Hammes. “Method for studying kinetics of light-induced transport across membranes.” Proc Natl Acad Sci U S A 78, no. 12 (December 1981): 7422–25. https://doi.org/10.1073/pnas.78.12.7422.
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  - Takabe, T., and G. G. Hammes. “pH dependence of adenosine 5'-triphosphate synthesis and hydrolysis catalyzed by reconstituted chloroplast coupling factor.” Biochemistry 20, no. 24 (November 24, 1981): 6859–64. https://doi.org/10.1021/bi00527a018.
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  - Bruist, M. F., and G. G. Hammes. “Further characterization of nucleotide binding sites on chloroplast coupling factor one.” Biochemistry 20, no. 22 (October 27, 1981): 6298–6305. https://doi.org/10.1021/bi00525a003.
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  - Dewey, T. G., and G. G. Hammes. “Steady state kinetics of ATP synthesis and hydrolysis catalyzed by reconstituted chloroplast coupling factor.” J Biol Chem 256, no. 17 (September 10, 1981): 8941–46.
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  - Cerione, R. A., and G. G. Hammes. “Nucleotide interactions with the dicyclohexylcarbodiimide-sensitive adenosinetriphosphatase from spinach chloroplasts.” Biochemistry 20, no. 12 (June 9, 1981): 3359–65. https://doi.org/10.1021/bi00515a008.
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  - Akiyama, S. K., and G. G. Hammes. “Elementary steps in the reaction mechanism of pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of flavin reduction.” Biochemistry 20, no. 6 (March 17, 1981): 1491–97. https://doi.org/10.1021/bi00509a013.
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  - Hammes, G. G. “Processing of intermediates in multienzyme complexes.” Biochem Soc Symp, no. 46 (1981): 73–90.
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  - Dewey, T. G., and G. G. Hammes. “Calculation on fluorescence resonance energy transfer on surfaces.” Biophys J 32, no. 3 (December 1980): 1023–35. https://doi.org/10.1016/S0006-3495(80)85033-8.
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  - Akiyama, S. K., and G. G. Hammes. “Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation.” Biochemistry 19, no. 18 (September 2, 1980): 4208–13. https://doi.org/10.1021/bi00559a011.
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  - Craig, D. W., and G. G. Hammes. “Structural mapping of rabbit muscle phosphofructokinase. Distance between the adenosine cyclic 3',5'-phosphate binding site and a reactive sulfhydryl group.” Biochemistry 19, no. 2 (January 22, 1980): 330–34. https://doi.org/10.1021/bi00543a013.
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  - Wolfman, N. M., and G. G. Hammes. “A calorimetric study of the interaction of ATP with rabbit muscle phosphofructokinase.” J Biol Chem 254, no. 24 (December 25, 1979): 12289–90.
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  - Angelides, K. J., and G. G. Hammes. “Structural and mechanistic studies of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli.” Biochemistry 18, no. 25 (December 11, 1979): 5531–37. https://doi.org/10.1021/bi00592a001.
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  - Carlier, M. F., D. A. Holowka, and G. G. Hammes. “Interaction of photoreactive and fluorescent nucleotides with chloroplast coupling factor 1.” Biochemistry 18, no. 16 (August 7, 1979): 3452–57. https://doi.org/10.1021/bi00583a003.
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  - Carlier, M. F., and G. G. Hammes. “Interaction of nucleotides with chloroplast coupling factor 1.” Biochemistry 18, no. 16 (August 7, 1979): 3446–51. https://doi.org/10.1021/bi00583a002.
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  - Baird, B. A., and G. G. Hammes. “Structure of oxidative- and photo-phosphorylation coupling factor complexes.” Biochim Biophys Acta 549, no. 1 (July 3, 1979): 31–53. https://doi.org/10.1016/0304-4173(79)90017-x.
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  - Angelides, K. J., S. K. Akiyama, and G. G. Hammes. “Subunit stoichiometry and molecular weight of the pyruvate dehydrogenase multienzyme complex from Escherichia coli.” Proc Natl Acad Sci U S A 76, no. 7 (July 1979): 3279–83. https://doi.org/10.1073/pnas.76.7.3279.
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  - Wolfman, N. M., A. C. Storer, and G. G. Hammes. “Temperature-jump study of the interaction of rabbit muscle phosphofructokinase with adenylyl imidodiphosphate and adenosine 5'-triphosphate.” Biochemistry 18, no. 12 (June 12, 1979): 2451–56. https://doi.org/10.1021/bi00579a003.
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  - Baird, B. A., U. Pick, and G. G. Hammes. “Structural investigation of reconstituted chloroplast ATPase with fluorescence measurements.” J Biol Chem 254, no. 10 (May 25, 1979): 3818–25.
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  - Angelides, K. J., and G. G. Hammes. “Fluorescence studies of the pyruvate dehydrogenase multienzyme complex from Escherichia coli.” Biochemistry 18, no. 7 (April 3, 1979): 1223–29. https://doi.org/10.1021/bi00574a017.
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  - Angelides, K. J., and G. G. Hammes. “Mechanism of action of the pyruvate dehydrogenase multienzyme complex from Escherichia coli.” Proc Natl Acad Sci U S A 75, no. 10 (October 1978): 4877–80. https://doi.org/10.1073/pnas.75.10.4877.
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  - Hahn, L. H., and G. G. Hammes. “Structural mapping of aspartate transcarbamoylase by fluorescence energy-transfer measurements: determination of the distance between catalytic sites of different subunits.” Biochemistry 17, no. 12 (June 13, 1978): 2423–29. https://doi.org/10.1021/bi00605a027.
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  - Goldhammer, A. R., and G. G. Hammes. “Steady-state kinetic study of rabbit muscle phosphofructokinase.” Biochemistry 17, no. 10 (May 16, 1978): 1818–1812. https://doi.org/10.1021/bi00603a002.
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  - Wolfman, N. M., W. R. Thompson, and G. G. Hammes. “Study of the interaction of adenylyl imidodiphosphate with rabbit muscle phosphofructokinase.” Biochemistry 17, no. 10 (May 16, 1978): 1813–17. https://doi.org/10.1021/bi00603a001.
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  - Holowka, D. A., and G. G. Hammes. “Chemical modification and fluorescence studies of chloroplast coupling factor.” Biochemistry 16, no. 25 (December 13, 1977): 5538–45. https://doi.org/10.1021/bi00644a023.
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  - Fan, S., A. C. Storer, and G. G. Hammes. “A proton and phosphorus nuclear magnetic resonance study of ternary complexes of cyclic adenosine 3':5'-monophosphate, adenosine 5'-triphosphate, and Mn2+.” J Am Chem Soc 99, no. 25 (December 7, 1977): 8293–98. https://doi.org/10.1021/ja00467a029.
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  - Shepherd, G. B., and G. G. Hammes. “Fluorescence energy transfer measurements in the pyruvate dehydrogenase multienzyme complex from Escherichia coli with chemically modified lipoic acid.” Biochemistry 16, no. 24 (November 29, 1977): 5234–41. https://doi.org/10.1021/bi00643a012.
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  - Lad, P. M., N. M. Wolfman, and G. G. Hammes. “Properties of rabbit muscle phosphofructokinase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole.” Biochemistry 16, no. 22 (November 1, 1977): 4802–6. https://doi.org/10.1021/bi00641a007.
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  - Wolfman, N. M., and G. G. Hammes. “Fluorescence energy transfer measurements in rabbit muscle phosphofructokinase.” Biochemistry 16, no. 22 (November 1, 1977): 4806–11. https://doi.org/10.1021/bi00641a008.
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  - Baird, B. A., and G. G. Hammes. “Chemical cross-linking studies of beef heart mitochondrial coupling factor 1.” J Biol Chem 252, no. 13 (July 10, 1977): 4743–48.
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  - Schlessinger, J., L. S. Barak, G. G. Hammes, K. M. Yamada, I. Pastan, W. W. Webb, and E. L. Elson. “Mobility and distribution of a cell surface glycoprotein and its interaction with other membrane components.” Proc Natl Acad Sci U S A 74, no. 7 (July 1977): 2909–13. https://doi.org/10.1073/pnas.74.7.2909.
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  - Papadakis, N., and G. G. Hammes. “Fluorescent derivatives of the pyruvate dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex.” Biochemistry 16, no. 9 (May 3, 1977): 1890–96. https://doi.org/10.1021/bi00628a020.
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  - Baird, B. A., and G. G. Hammes. “Chemical cross-linking studies of chloroplast coupling factor 1.” J Biol Chem 251, no. 22 (November 25, 1976): 6953–62.
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  - Hammes, G. G., and M. Rodbell. “Simple model for hormone-activated adenylate cyclase systems.” Proc Natl Acad Sci U S A 73, no. 4 (April 1976): 1189–92. https://doi.org/10.1073/pnas.73.4.1189.
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  - Koren, R., and G. G. Hammes. “A kinetic study of protein-protein interactions.” Biochemistry 15, no. 5 (March 9, 1976): 1165–71. https://doi.org/10.1021/bi00650a032.
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  - Parr, G. R., and G. G. Hammes. “A kinetic study of the subunit dissociation and reassembly of rabbit muscle phosphofructokinase.” Biochemistry 15, no. 4 (February 24, 1976): 857–62. https://doi.org/10.1021/bi00649a020.
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  - Shepherd, G. B., and G. G. Hammes. “Fluorescence energy transfer measurements between ligand binding sites of the pyruvate dehydrogenase multienzyme complex.” Biochemistry 15, no. 2 (January 27, 1976): 311–17. https://doi.org/10.1021/bi00647a011.
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  - Cantley, L. C., and G. G. Hammes. “Investigation of quercetin binding sites on chloroplast coupling factor 1.” Biochemistry 15, no. 1 (January 13, 1976): 1–8. https://doi.org/10.1021/bi00646a001.
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  - Cantley, L. C., and G. G. Hammes. “Characterization of sulfhydryl groups on chloroplast coupling factor 1 exposed by heat activation.” Biochemistry 15, no. 1 (January 13, 1976): 9–14. https://doi.org/10.1021/bi00646a002.
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  - Telford, J. N., P. M. Lad, and G. G. Hammes. “Electron microscope study of native and crosslinked rabbit muscle phosphofructokinase.” Proc Natl Acad Sci U S A 72, no. 8 (August 1975): 3054–56. https://doi.org/10.1073/pnas.72.8.3054.
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  - Cantley, L. C., and G. G. Hammes. “Characterization of nucleotide binding sites on chloroplast coupling factor 1.” Biochemistry 14, no. 13 (July 1975): 2968–75. https://doi.org/10.1021/bi00684a027.
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  - Cantley, L. C., and G. G. Hammes. “Fluorescence energy transfer between ligand binding sites on chloroplast coupling factor 1.” Biochemistry 14, no. 13 (July 1975): 2976–81. https://doi.org/10.1021/bi00684a028.
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  - Fan, S., L. W. Harrison, and G. G. Hammes. “Nuclear magnetic resonance study of ligand binding to Mn-aspartate transcarbamylase.” Biochemistry 14, no. 10 (May 20, 1975): 2219–24. https://doi.org/10.1021/bi00681a027.
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  - Parr, G. R., and G. G. Hammes. “Subunit dissociation and unfolding of rabbit muscle phosphofructokinase by guanidine by hydrochloride.” Biochemistry 14, no. 8 (April 22, 1975): 1600–1605. https://doi.org/10.1021/bi00679a009.
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  - Koren, R., and G. G. Hammes. “Interaction of reduced nicotinamide adenine dinucleotide with beef heart s-malate dehydrogenase.” Biochemistry 14, no. 5 (March 11, 1975): 1021–25. https://doi.org/10.1021/bi00676a021.
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  - Hill, D. E., and G. G. Hammes. “An equilibrium binding study of the interaction of fructose 6-phosphate and fructose 1,6-bisphosphate with rabbit muscle phosphofructokinase.” Biochemistry 14, no. 2 (January 28, 1975): 203–13. https://doi.org/10.1021/bi00673a003.
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  - Matsumoto, S., and G. G. Hammes. “Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase.” Biochemistry 14, no. 2 (January 28, 1975): 214–24. https://doi.org/10.1021/bi00673a004.
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  - Grover, A. K., A. J. Slotboom, G. H. de Haas, and G. G. Hammes. “Lipid specificity of beta-hydroxybutyrate dehydrogenase activation.” J Biol Chem 250, no. 1 (January 10, 1975): 31–38.
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  - Lad, P. M., and G. G. Hammes. “Physical and chemical properties of rabbit muscle phosphofructokinase cross-linked with dimethyl suberimidate.” Biochemistry 13, no. 22 (October 22, 1974): 4530–37. https://doi.org/10.1021/bi00719a009.
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  - Hantgan, R. R., G. G. Hammes, and H. A. Scheraga. “Pathways of folding of reduced bovine pancreatic ribonuclease.” Biochemistry 13, no. 17 (August 13, 1974): 3421–31. https://doi.org/10.1021/bi00714a001.
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  - Grover, A. K., and G. G. Hammes. “Affinity chromatography of beta-hydroxybutyrate dehydrogenase on Nad and hydrophobic chain derivatives of sepharose.” Biochim Biophys Acta 356, no. 3 (August 9, 1974): 309–18. https://doi.org/10.1016/0005-2736(74)90271-5.
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  - Tondre, C., and G. G. Hammes. “Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates.” Biochemistry 13, no. 15 (July 16, 1974): 3131–36. https://doi.org/10.1021/bi00712a020.
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  - Moe, O. A., D. A. Lerner, and G. G. Hammes. “Fluorescence energy transfer between the thiamine diphosphate and flavine adenine dinucleotide binding sites on the pyruvate dehydrogenase multienzyme complex.” Biochemistry 13, no. 12 (June 4, 1974): 2552–57. https://doi.org/10.1021/bi00709a012.
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  - Moe, O. A., and G. G. Hammes. “A study of the binding of thiamine diphosphate and thiochrome diphosphate to the pyruvate dehydrogenase multienzyme complex.” Biochemistry 13, no. 12 (June 4, 1974): 2547–52. https://doi.org/10.1021/bi00709a011.
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  - Hammes, G. G., and C. W. Wu. “Kinetics of allosteric enzymes.” Annu Rev Biophys Bioeng 3, no. 0 (1974): 1–33. https://doi.org/10.1146/annurev.bb.03.060174.000245.
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  - Cantley, L. C., and G. G. Hammes. “Activation of beef heart mitochondrial adenosine triphosphatase by 2,4-dinitrophenol.” Biochemistry 12, no. 24 (November 20, 1973): 4900–4904. https://doi.org/10.1021/bi00748a014.
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  - Lad, P. M., D. E. Hill, and G. G. Hammes. “Influence of allosteric ligands on the activity and aggregation of rabbit muscle phosphofructokinase.” Biochemistry 12, no. 22 (October 23, 1973): 4303–9. https://doi.org/10.1021/bi00746a001.
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  - Tondre, C., and G. G. Hammes. “A kinetic study of the binding of an ADP fluorescent analog to mitochondrial ATPase.” Biochim Biophys Acta 314, no. 2 (August 31, 1973): 245–49. https://doi.org/10.1016/0005-2728(73)90139-4.
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  - Menzel, H. M., and G. G. Hammes. “Purification and characterization of a lecithin-D(-)- -hydroxybutyrate dehydrogenase complex.” J Biol Chem 248, no. 14 (July 25, 1973): 4885–89.
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  - Hammes, G. G. “Receptor biophysics and biochemistry. Enzymes.” Neurosci Res Program Bull 11, no. 3 (June 1973): 164–75.
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  - Hilborn, D. A., L. W. Harrison, and G. G. Hammes. “An on-line computer system for the acquisition and analysis of temperature jump data.” Comput Biomed Res 6, no. 3 (June 1973): 216–27. https://doi.org/10.1016/0010-4809(73)90036-0.
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  - Harrison, L. W., and G. G. Hammes. “Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5'-triphosphate.” Biochemistry 12, no. 7 (March 27, 1973): 1395–1400. https://doi.org/10.1021/bi00731a020.
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  - Matsumoto, S., and G. G. Hammes. “An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate.” Biochemistry 12, no. 7 (March 27, 1973): 1388–94. https://doi.org/10.1021/bi00731a019.
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  - Pavelich, M. J., and G. G. Hammes. “Aggregation of rabbit muscle phosphofructokinase.” Biochemistry 12, no. 7 (March 27, 1973): 1408–14. https://doi.org/10.1021/bi00731a022.
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  - Wu, C. W., and G. G. Hammes. “Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analog.” Biochemistry 12, no. 7 (March 27, 1973): 1400–1408. https://doi.org/10.1021/bi00731a021.
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  - Hilborn, D. A., and G. G. Hammes. “Equilibrium binding of nucleotides to beef heart mitochondrial adenosine triphosphatase.” Biochemistry 12, no. 5 (February 27, 1973): 983–90. https://doi.org/10.1021/bi00729a030.
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  - Hammes, G. G., P. J. Lillford, and J. Simplicio. “Mechanism of nicotinamide-adenine dinucleotide binding to rabbit muscle glyceraldehyde 3-phosphate dehydrogenase.” Biochemistry 10, no. 20 (September 28, 1971): 3686–93. https://doi.org/10.1021/bi00796a008.
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  - Hammes, G. G., and C. W. Wu. “Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria.” Science 172, no. 3989 (June 18, 1971): 1205–11. https://doi.org/10.1126/science.172.3989.1205.
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  - Hammes, G. G., and C. W. Wu. “Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria.” Science (New York, N.Y.) 172, no. 989 (June 1971): 1205–11.
  - Hammes, G. G., and D. A. Hilborn. “Steady state kinetics of soluble and membrane-bound mitochondrial ATPase.” Biochim Biophys Acta 233, no. 3 (June 1, 1971): 580–90. https://doi.org/10.1016/0005-2736(71)90156-8.
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  - Hammes, G. G., and C. W. Wu. “Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate.” Biochemistry 10, no. 11 (May 25, 1971): 2150–56. https://doi.org/10.1021/bi00787a030.
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  - Faeder, E. J., and G. G. Hammes. “Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme.” Biochemistry 10, no. 6 (March 16, 1971): 1041–45. https://doi.org/10.1021/bi00782a016.
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  - Hammes, G. G., R. W. Porter, and G. R. Stark. “Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate.” Biochemistry 10, no. 6 (March 16, 1971): 1046–50. https://doi.org/10.1021/bi00782a017.
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  - Hammes, G. G., and C. W. Wu. “Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs.” Biochemistry 10, no. 6 (March 16, 1971): 1051–57. https://doi.org/10.1021/bi00782a018.
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  - Hammes, G. G., and D. E. Tallman. “A nuclear magnetic resonance study of the interaction of L-epinephrine with phospholipid vesicles.” Biochim Biophys Acta 233, no. 1 (March 9, 1971): 17–25. https://doi.org/10.1016/0005-2736(71)90353-1.
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  - Del Rosario, E. J., and G. G. Hammes. “Temperature-jump study of the interaction of malate dehydrogenase with reduced nicotinamide-adenine dinucleotide and D-malate.” Biochemistry 10, no. 4 (February 16, 1971): 716–20. https://doi.org/10.1021/bi00780a025.
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  - Faeder, E. J., and G. G. Hammes. “Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit.” Biochemistry 9, no. 21 (October 13, 1970): 4043–49. https://doi.org/10.1021/bi00823a003.
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  - Hammes, G. G., and D. E. Tallman. “Application of the temperature-jump technique to the study of phospholipid dispersions.” J Am Chem Soc 92, no. 20 (October 7, 1970): 6042–46. https://doi.org/10.1021/ja00723a038.
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  - Hammes, G. G., and J. Simplicio. “Relaxation spectra of pyruvate kinase.” Biochim Biophys Acta 212, no. 3 (September 16, 1970): 428–33. https://doi.org/10.1016/0005-2744(70)90248-2.
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  - Eckfeldt, J., G. G. Hammes, S. C. Mohr, and C. W. Wu. “Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit.” Biochemistry 9, no. 17 (August 18, 1970): 3353–62. https://doi.org/10.1021/bi00819a010.
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  - Hammes, G. G., R. W. Porter, and C. W. Wu. “Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase.” Biochemistry 9, no. 15 (July 21, 1970): 2992–94. https://doi.org/10.1021/bi00817a009.
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  - Hammes, G. G., and S. E. Schullery. “Structure of macromolecular aggregates. II. Construction of model membranes from phospholipids and polypeptides.” Biochemistry 9, no. 13 (June 23, 1970): 2555–63. https://doi.org/10.1021/bi00815a001.
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  - Hammes, G. G., and P. B. Roberts. “Ultrasonic attenuation measurements in phospholipid dispersions.” Biochim Biophys Acta 203, no. 2 (April 21, 1970): 220–27. https://doi.org/10.1016/0005-2736(70)90135-5.
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  - Del Rosario, E. J., and G. G. Hammes. “Relaxation spectra of ribonuclease. VII. The interaction of ribonuclease with uridine 2',3'-cyclic phosphate.” J Am Chem Soc 92, no. 6 (March 25, 1970): 1750–53. https://doi.org/10.1021/ja00709a056.
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  - Hammes, G. G., and F. G. Walz. “Kinetic properties of iodinated ribonuclease A.” Biochim Biophys Acta 198, no. 3 (March 18, 1970): 604–6. https://doi.org/10.1016/0005-2744(70)90138-5.
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  - Rosario, E. J. del, and G. G. Hammes. “Kinetic and equilibrium studies of the ribonuclease-catalyzed hydrolysis of uridine 2',3'-cyclic phosphate.” Biochemistry 8, no. 5 (May 1969): 1884–89. https://doi.org/10.1021/bi00833a017.
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  - Hammes, G. G., and J. L. Haslam. “A kinetic investigation of the interaction of erythro-beta-hydroxyaspartic acid with aspartate aminotransferase.” Biochemistry 8, no. 4 (April 1969): 1591–98. https://doi.org/10.1021/bi00832a040.
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  - Hammes, G. G., and P. B. Roberts. “Dynamics of the helix--coil transition in poly-L-ornithine.” J Am Chem Soc 91, no. 7 (March 26, 1969): 1812–16. https://doi.org/10.1021/ja01035a036.
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  - Hammes, G. G., and J. K. Hurst. “Relaxation spectra of adenosine triphosphate-creatine phosphotransferase.” Biochemistry 8, no. 3 (March 1969): 1083–94. https://doi.org/10.1021/bi00831a040.
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  - Swann, J. C., and G. G. Hammes. “Sel-association of glucagon. Equilibrium studies.” Biochemistry 8, no. 1 (January 1969): 1–7. https://doi.org/10.1021/bi00829a001.
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  - Hammes, G. G., and S. E. Schullery. “Structure of macromolecular aggregates. I. Aggregation-induced conformational changes in polypeptides.” Biochemistry 7, no. 11 (November 1968): 3882–87. https://doi.org/10.1021/bi00851a014.
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  - Hammes, G. G., and A. C. Park. “Kinetic studies of hydrogen bonding. 1-Cyclohexyluracil and 9-ethyladenine.” J Am Chem Soc 90, no. 15 (July 17, 1968): 4151–57. https://doi.org/10.1021/ja01017a042.
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  - Hammes, G. G., and C. N. Pace. “Ultrasonic absorption measurements in aqueous solutions of glycine, diglycine, and triglycine.” J Phys Chem 72, no. 6 (June 1968): 2227–30. https://doi.org/10.1021/j100852a060.
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  - Anderson, D. G., G. G. Hammes, and F. G. Walz. “Binding of phosphate ligands to ribonuclease A.” Biochemistry 7, no. 5 (May 1968): 1637–45. https://doi.org/10.1021/bi00845a004.
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  - Hammes, G. G., and J. L. Haslam. “A kinetic investigation of the interaction of alpha-methylaspartic acid with aspartate aminotransferase.” Biochemistry 7, no. 4 (April 1968): 1519–25. https://doi.org/10.1021/bi00844a039.
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  - Hammes, G. G. “Relaxation spectrometry of biological systems.” Adv Protein Chem 23 (1968): 1–57. https://doi.org/10.1016/s0065-3233(08)60399-x.
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  - Hammes, G. G., and J. F. Tancredi. “Thermodynamic parameters of the alpha-methyl aspartate-aspartate aminotransferase interaction.” Biochim Biophys Acta 146, no. 1 (September 12, 1967): 312–13. https://doi.org/10.1016/0005-2744(67)90104-0.
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  - Fasella, P., and G. G. Hammes. “A temperature jump study of aspartate aminotransferase. a reinvestigation.” Biochemistry 6, no. 6 (June 1967): 1798–1804. https://doi.org/10.1021/bi00858a031.
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  - Hammes, G. G., and J. C. Swann. “Influence of denaturing agents on solvent structure.” Biochemistry 6, no. 6 (June 1967): 1591–96. https://doi.org/10.1021/bi00858a004.
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  - Hammes, G. G., and P. R. Schimmel. “Relaxation spectra of enzymatic reactions.” J Phys Chem 71, no. 4 (March 1967): 917–23. https://doi.org/10.1021/j100863a023.
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  - Erman, J. E., and G. G. Hammes. “Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2':3'-cyclic phosphate.” J Am Chem Soc 88, no. 23 (December 5, 1966): 5607–14. https://doi.org/10.1021/ja00975a046.
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  - Erman, J. E., and G. G. Hammes. “Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3':5'-cytidine.” J Am Chem Soc 88, no. 23 (December 5, 1966): 5614–17. https://doi.org/10.1021/ja00975a047.
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  - Hammes, G. G., and H. A. Scheraga. “A model of ribonuclease based on chemical evidence.” Biochemistry 5, no. 11 (November 1966): 3690–93. https://doi.org/10.1021/bi00875a044.
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  - Hammes, G. G., and H. O. Spivey. “A kinetic study of the hydrogen-bond dimerization of 2-pyridone.” J Am Chem Soc 88, no. 8 (April 20, 1966): 1621–25. https://doi.org/10.1021/ja00960a006.
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  - Fasella, P., A. Giartosio, and G. G. Hammes. “The interaction of aspartate aminotransferase with alpha-methylaspartic acid.” Biochemistry 5, no. 1 (January 1966): 197–202. https://doi.org/10.1021/bi00865a026.
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  - Cathou, R. E., G. G. Hammes, and P. R. Schimmel. “Optical rotatory dispersion of ribonuclease and ribonuclease--nucleotide complexes.” Biochemistry 4, no. 12 (December 1965): 2687–90. https://doi.org/10.1021/bi00888a018.
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  - Cathou, R. E., and G. G. Hammes. “Relaxation spectra of ribonuclease. 3. Further investigation of the interaction of ribonuclease and cytidine 3'-phosphate.” J Am Chem Soc 87, no. 21 (November 5, 1965): 4674–80. https://doi.org/10.1021/ja00949a003.
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  - French, T. C., and G. G. Hammes. “Relaxation spectra of ribonuclease. II. Isomerization of ribonuclease at neutral pH values.” J Am Chem Soc 87, no. 21 (November 5, 1965): 4669–73. https://doi.org/10.1021/ja00949a002.
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  - Hammes, G. G., and P. R. Schimmel. “Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease.” J Am Chem Soc 87, no. 21 (November 5, 1965): 4665–69. https://doi.org/10.1021/ja00949a001.
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  - Fasella, P., G. G. Hammes, and P. R. Schimmel. “A Sephadex dialysis method of determining small molecule-macromolecule binding constants.” Biochim Biophys Acta 103, no. 4 (August 10, 1965): 708–10. https://doi.org/10.1016/0005-2787(65)90094-8.
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  - BAHR, J. T., R. E. CATHOU, and G. G. HAMMES. “A THERMODYNAMIC STUDY OF THE HYDROLYSIS OF CYTIDINE 2',3'-CYCLIC PHOSPHATE.” J Biol Chem 240 (August 1965): 3372–78.
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  - BURKE, J. J., G. G. HAMMES, and T. B. LEWIS. “ULTRASONIC ATTENUATION MEASUREMENTS IN POLY-L-GLUAMIC ACID SOLUTIONS.” J Chem Phys 42 (May 15, 1965): 3520–25. https://doi.org/10.1063/1.1695754.
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  - FASELLA, P., and G. G. HAMMES. “ULTRAVIOLET ROTATORY DISPERSION OF ASPARTIC AMINOTRANSFERASE.” Biochemistry 4 (May 1965): 801–5. https://doi.org/10.1021/bi00881a002.
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  - FASELLA, P., and G. G. HAMMES. “A CORRELATION BETWEEN THE PROTEIN STRUCTURE AND CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE.” Biochim Biophys Acta 92 (December 23, 1964): 630–32. https://doi.org/10.1016/0926-6569(64)90030-6.
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  - HAMMES, G. G. “MECHANISM OF ENZYME CATALYSIS.” Nature 204 (October 24, 1964): 342–43. https://doi.org/10.1038/204342a0.
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  - HAMMES, G. G., and S. A. LEVISON. “A KINETIC INVESTIGATION OF THE INTERACTION OF ADENOSINE-5'-TRIPHOSPHATE WITH DIVALENT METAL IONS.” Biochemistry 3 (October 1964): 1504–6. https://doi.org/10.1021/bi00898a019.
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  - FASELLA, P., and G. G. HAMMES. “AN OPTICAL ROTATORY DISPERSION STUDY OF ASPARTIC AMINO TRANSFERASE.” Biochemistry 3 (April 1964): 530–35. https://doi.org/10.1021/bi00892a011.
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  - FASELLA, P., and G. G. HAMMES. “Studies of the enzyme hexokinase. IV. The role of sulfhydryl groups.” Arch Biochem Biophys 100 (February 1963): 295–97. https://doi.org/10.1016/0003-9861(63)90075-4.
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  - EIGEN, M., and G. G. HAMMES. “ELEMENTARY STEPS IN ENZYME REACTIONS (AS STUDIED BY RELAXATION SPECTROMETRY).” Adv Enzymol Relat Subj Biochem 25 (1963): 1–38. https://doi.org/10.1002/9780470122709.ch1.
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  - FASELLA, P., G. G. HAMMES, and B. L. VALLEE. “Concerning the role of metals in enzymic transamination.” Biochim Biophys Acta 65 (November 19, 1962): 142–43. https://doi.org/10.1016/0006-3002(62)90158-0.
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  - DIEBLER, H., M. EIGEN, and G. G. HAMMES. “[Relaxation spectrometric studies of fast reactions of ATP in aqueous solution].” Z Naturforsch B 15B (September 1960): 554–60.
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