Premium
Control of peptide conformation by the Thorpe‐Ingold effect (C α ‐tetrasubstitution)
Author(s) -
Toniolo Claudio,
Crisma Marco,
Formaggio Fernando,
Peggion Cristina
Publication year - 2001
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 - 10.1002/1097-0282(2001)60:6<396::aid-bip10184>3.0.co;2-7
Subject(s) - chemistry , chirality (physics) , peptide , stereochemistry , amino acid , helix (gastropod) , crystallography , side chain , alpha (finance) , crystal structure , alpha helix , circular dichroism , organic chemistry , chiral symmetry , biochemistry , snail , ecology , biology , quark , polymer , quantum mechanics , nambu–jona lasinio model , physics , patient satisfaction , construct validity , medicine , nursing
The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by conformational energy computations, crystal‐state (x‐ray diffraction) analyses, and solution ( 1 H‐NMR and spectroscopic) investigations, are reviewed. It is concluded that 3 10 /α‐helical structures and the fully extended (C 5 ) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C α i↔ C α icyclized) of their side chains. The intriguing relationship between α‐carbon chirality and bend/helix handedness is also illustrated. γ‐Bends and semiextended conformations are rarely observed. Formation of β‐sheet structures is prevented. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 396–419, 2001