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Fluorine in a Native Protein Environment—How the Spatial Demand and Polarity of Fluoroalkyl Groups Affect Protein Folding
Author(s) -
Jäckel Christian,
Salwiczek Mario,
Koksch Beate
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200504387
Subject(s) - steric effects , folding (dsp implementation) , alkyl , side chain , chemistry , polarity (international relations) , protein folding , affect (linguistics) , fluorine , amino acid , hydrophobic effect , organic chemistry , biophysics , biochemistry , psychology , biology , communication , polymer , electrical engineering , cell , engineering
Give and take : The influence of fluoro substitution of amino acid side chains on their interaction profile in a native polypeptide environment was studied systematically. The fluorination of alkyl groups has opposing electrostatic and steric consequences for the stability of hydrophobic protein cores.