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Peptides as Conformational Switch: Medium‐Induced Conformational Transitions of Designed Peptides
Author(s) -
Mutter Manfred,
Hersperger René
Publication year - 1990
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199001851
Subject(s) - oligopeptide , amphiphile , chemistry , helix (gastropod) , peptide , conformational change , stereochemistry , biophysics , biochemistry , biology , organic chemistry , polymer , ecology , snail , copolymer
The synthetic oligopeptide I undergoes a spontaneous, reversible transition from an α‐helix to a β‐sheet structure in mixtures of 45% 2,2,2‐trifluoroethanol and 55% H 2 O. The amphiphilic oligopeptide 1 and two isomers were expressly designed for this investigation. Such peptides, which can exist in several conformations, might find application as “switches” in the de novo design of artificial proteins.