The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Amino Acid Preferences for Specific Locations at the Ends of α Helices
Abstract
A definition based on α-carbon positions and a sample of 215 α helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.
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Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
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Metadata
- Authors
- Richardson, J. S., & Richardson, D. C.
- Venue
- Science
- Published
- 1988-06-17
- Volume
- 240
- Issue
- 4859
- Pages
- 1648-1652
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2081359387
- Cited by
- 1,364
- References
- 2
- FWCI
- 18.42
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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