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Conformational preferences of side‐chain protected amino acid residues and their impact in peptide synthesis
Author(s) -
Maser F.,
Klein B.,
Mutter M.,
Toniolo C.,
Bonora G. M.
Publication year - 1983
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/bip.360220132
Subject(s) - chemistry , side chain , peptide , amino acid , solubility , amino acid residue , stereochemistry , helix (gastropod) , peptide sequence , combinatorial chemistry , biochemistry , organic chemistry , polymer , ecology , biology , snail , gene
Using the host‐guest technique, tentative scales for the helix‐inducing power and the β‐structure‐forming potential of various side‐chain protected amino acid residues in trifluoro‐ethanol are established mainly by CD measurements. The generally lower tendency for β‐structure formation of the host–guest peptides compared to that of the host peptide is discussed. The influence of these conformational features on the solubility of the peptides is also pointed out.