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Side‐chain control of folding of the homologous α‐, β‐, and γ‐peptides into “mixed” helices (β‐helices)
Author(s) -
Baldauf Carsten,
Günther Robert,
Hofmann HansJörg
Publication year - 2005
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20249
Subject(s) - chemistry , substituent , folding (dsp implementation) , helix (gastropod) , homologous series , peptide , crystallography , collagen helix , ab initio , stereochemistry , triple helix , biochemistry , organic chemistry , ecology , snail , electrical engineering , biology , engineering
A systematic analysis of the substituent influence on the formation of the unique secondary structure type of “mixed” helices in the homologous α‐, β‐, and γ‐peptides was performed on the basis of ab initio molecular orbital theory. Contrary to the common periodic peptide helices, mixed helices have an alternating periodicity and their hydrogen‐bonding pattern is similar to those of β‐sheets. They belong, therefore, to the family of β‐helices. It is shown that folding of peptide sequences into mixed helices is energetically preferred over folding into their periodic counterparts in numerous cases. The influence of entropy and solvents on the formation of the various competitive mixed and periodic helix types is discussed. Among the oligomers of the various homologous amino acids, β‐peptides show the highest tendency to form β‐helices. The rules of substituent influence derived from the analysis of a wide variety of backbone substitution patterns might be helpful for a rational design of mixed helix structures, which could be important for mimicking membrane channels. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 80: 675–687, 2005 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com