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The Influence of Two‐Dimensional Organization on Peptide Conformation
Author(s) -
White Simon J.,
Johnson Steven D.,
Sellick Mark A.,
Bronowska Agnieszka,
Stockley Peter G.,
Wälti Christoph
Publication year - 2015
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.201408971
Subject(s) - monolayer , circular dichroism , random coil , peptide , chemistry , molecular dynamics , molecule , molecular model , conformational change , biophysics , ionic bonding , crystallography , chemical physics , stereochemistry , computational chemistry , biochemistry , ion , biology , organic chemistry
Molecular crowding plays a significant role in regulating molecular conformation in cellular environments. It is also likely to be important wherever high molecular densities are required, for example in surface‐phase studies, in which molecular densities generally far exceed those observed in solution. Using on‐surface circular dichroism (CD) spectroscopy, we have investigated the structure of a synthetic peptide assembled into a highly packed monolayer. The immobilized peptide undergoes a structural transition between α‐helical and random coil conformation upon changes in pH and ionic concentration, but critically the threshold for conformational change is altered dramatically by molecular crowding within the peptide monolayer. This study highlights the often overlooked role molecular crowding plays in regulating molecular structure and function in surface‐phase studies of biological molecules.