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Basic conformers in β‐peptides
Author(s) -
Möhle Kerstin,
Günther Robert,
Thormann Michael,
Sewald Norbert,
Hofmann HansJörg
Publication year - 1999
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199908)50:2<167::aid-bip6>3.0.co;2-m
Subject(s) - chemistry , peptide , conformational isomerism , ab initio , amino acid , monomer , computational chemistry , molecular orbital , protein secondary structure , force field (fiction) , molecular model , stereochemistry , molecule , crystallography , organic chemistry , polymer , biochemistry , artificial intelligence , computer science
The conformation of oligomers of β‐amino acids of the general type Ac‐[β‐Xaa] n ‐NHMe (β‐Xaa = β‐Ala, β‐Aib, and β‐Abu; n = 1–4) was systematically examined at different levels of ab initio molecular orbital theory (HF/6‐31G*, HF/3‐21G). The solvent influence was considered employing two quantum‐mechanical self‐consistent reaction field models. The results show a wide variety of possibilities for the formation of characteristic elements of secondary structure in β‐peptides. Most of them can be derived from the monomer units of blocked β‐peptides with n = 1. The stability and geometries of the β‐peptide structures are considerably influenced by the side‐chain positions, by the configurations at the C α ‐ and C β ‐atoms of the β‐amino acid constituents, and especially by environmental effects. Structure peculiarities of β‐peptides, in particular those of various helix alternatives, are discussed in relation to typical elements of secondary structure in α‐peptides. © 1999 John Wiley & Sons, Inc. Biopoly 50: 167–184, 1999