Gordon G. Hammes

Journal article Proc Natl Acad Sci U S A · October 15, 2002 Featured Work The thermodynamics and kinetics of the interaction of dihydrofolate reductase (DHFR) with methotrexate have been studied by using fluorescence, stopped-flow, and single-molecule methods. DHFR was modified to permit the covalent addition of a fluorescent mo ... Full text Link to item Cite

Multiple conformational changes in enzyme catalysis.

Journal article Biochemistry · July 2, 2002 Featured Work Understanding the molecular mechanisms of enzyme catalysis and allosteric regulation has been a primary goal of biochemistry for many years. The dynamics of these processes, approached through a variety of kinetic methods, are discussed. The results obtain ... Full text Link to item Cite

A golden era for understanding enzyme mechanisms.

Journal article Protein Sci · March 1998 Featured Work Full text Link to item Cite

Transient kinetic approaches to enzyme mechanisms.

Journal article Methods Enzymol · 1995 Featured Work Full text Link to item Cite

Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles.

Journal article Biochemistry · October 23, 1990 Featured Work The spatial relationship of specific sites on chloroplast coupling factor, reconstituted in asolectin vesicles, to the bilayer surface has been studied with fluorescence methods. Fluorescence resonance energy transfer measurements have been used to map the ... Full text Link to item Cite

Rotational dynamics of chloroplast ATP synthase in phospholipid vesicles.

Journal article Biochemistry · April 3, 1990 Featured Work The rotational dynamics of the purified dicyclohexylcarbodiimide-sensitive H(+)-ATPase (DSA) reconstituted into phospholipid vesicles and of the DSA coreconstituted with the proton pump bacterio-rhodopsin were examined by using the technique of time-resolv ... Full text Link to item Cite

The ATP binding site of the yeast plasma membrane proton-translocating ATPase.

Journal article J Biol Chem · January 25, 1990 Featured Work Photoaffinity labeling of the active site of the yeast plasma membrane H(+)-ATPase has been studied with 2-azido-AMP and 2-azido-ATP. The ATPase activity of the enzyme decreases as the time of photolysis of the photoactive nucleotides in the presence of th ... Link to item Cite