Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.
Publication
, Journal Article
Oas, TG; McIntosh, LP; O'Shea, EK; Dahlquist, FW; Kim, PS
Published in: Biochemistry
March 27, 1990
Previous work has shown that a synthetic peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 forms a stable dimer of alpha-helices and that the helices are oriented in a parallel manner. Two-dimensional nuclear magnetic resonance spectroscopy (NMR) is used here to demonstrate that the helix is continuous for at least 32 of the 33 residues in the peptide. The results also indicate that the dimer is symmetric. It is therefore unlikely that the interdigitation model for the structure of leucine zippers is correct, since interdigitation of leucine residues in a parallel dimer would lead to an asymmetric structure. The data are consistent with a coiled-coil structure.
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Published In
Biochemistry
DOI
ISSN
0006-2960
Publication Date
March 27, 1990
Volume
29
Issue
12
Start / End Page
2891 / 2894
Location
United States
Related Subject Headings
- Transcription Factors
- Saccharomyces cerevisiae Proteins
- Protein Kinases
- Protein Conformation
- Peptides
- Molecular Sequence Data
- Models, Structural
- Magnetic Resonance Spectroscopy
- Leucine
- Kinetics
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Oas, T. G., McIntosh, L. P., O’Shea, E. K., Dahlquist, F. W., & Kim, P. S. (1990). Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry, 29(12), 2891–2894. https://doi.org/10.1021/bi00464a001
Oas, T. G., L. P. McIntosh, E. K. O’Shea, F. W. Dahlquist, and P. S. Kim. “Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.” Biochemistry 29, no. 12 (March 27, 1990): 2891–94. https://doi.org/10.1021/bi00464a001.
Oas TG, McIntosh LP, O’Shea EK, Dahlquist FW, Kim PS. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 1990 Mar 27;29(12):2891–4.
Oas, T. G., et al. “Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.” Biochemistry, vol. 29, no. 12, Mar. 1990, pp. 2891–94. Pubmed, doi:10.1021/bi00464a001.
Oas TG, McIntosh LP, O’Shea EK, Dahlquist FW, Kim PS. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 1990 Mar 27;29(12):2891–2894.
Published In
Biochemistry
DOI
ISSN
0006-2960
Publication Date
March 27, 1990
Volume
29
Issue
12
Start / End Page
2891 / 2894
Location
United States
Related Subject Headings
- Transcription Factors
- Saccharomyces cerevisiae Proteins
- Protein Kinases
- Protein Conformation
- Peptides
- Molecular Sequence Data
- Models, Structural
- Magnetic Resonance Spectroscopy
- Leucine
- Kinetics