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Pseudo‐prolines: Induction of cis/trans ‐conformational interconversion by decreased transition state barriers
Author(s) -
Mutter Manfred,
Wöhr Torsten,
Gioria Séverine,
Keller Michael
Publication year - 1999
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/(sici)1097-0282(1999)51:2<121::aid-bip2>3.0.co;2-o
Subject(s) - chemistry , isomerization , molecular dynamics , amide , transition state theory , kinetics , transition state , helix (gastropod) , hydrogen bond , stereochemistry , limiting , peptide bond , molecule , computational chemistry , peptide , reaction rate constant , catalysis , organic chemistry , biochemistry , mechanical engineering , ecology , physics , quantum mechanics , snail , engineering , biology
Molecular events such as cis/trans isomerization of Xaa‐Pro tertiary amide bonds in peptides and proteins are slow on the overall time scale of the formation of a final biostructure and are, therefore, rate limiting. In order to pursue a better understanding of the molecular events underlying such slow interconversions, we applied the recently introduced pseudo‐proline (ΨPro) concept as a tool to study the dynamics of Xaa‐Pro bonds by determining the kinetics and thermodynamics of cis/trans isomerism. We show that enhanced isomerization rates of tertiary amide bonds prior to a ΨPro unit in short model peptides is due to lowered transition state barriers. In addition, pronounced effects upon the dynamics of the reversible transition between helix I and II of oligoprolines containing one or several ΨPro units were observed. © 1999 John Wiley & Sons, Inc. Biopoly 51: 121–128, 1999