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- W2022125630 abstract "An analysis of 636 helical segments, ranging in length from 4 to 32 residues, from 123 independent protein crystal structures reveals that helix termination by residues in left handed (α L ) helical conformations is a common occurrence. Gly and Asn residues are the most frequent α L helix terminators, with the former having a very high propensity to adopt such conformations. The α R ‐α R ‐α R ‐α L segment at the C termini of protein helices often possesses a 6 → 1 (π‐type) hydrogen bond between the CO of residue i and the NH of residue i + 5 with residue i + 4 occurring in the α L conformation. A stereochemical analysis of 216 examples shows that in 62 cases the 6 → 1 hydrogen bond is absent. The present analysis provides a quantitative measure of the propensity of the 20 amino acids to adopt α L helix terminating conformations." @default.
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- W2022125630 date "1993-04-19" @default.
- W2022125630 modified "2023-10-16" @default.
- W2022125630 title "Termination of right handed helices in proteins by residues in left handed helical conformations" @default.
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- W2022125630 doi "https://doi.org/10.1016/0014-5793(93)80625-5" @default.
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