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Details of the Partial Unfolding of T4 Lysozyme on Quartz Using Site‐Directed Spin Labeling
Author(s) -
Jacobsen Kerstin,
Hubbell Wayne L.,
Ernst Oliver P.,
Risse Thomas
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.200600008
Subject(s) - ionic strength , lysozyme , quartz , chemistry , crystallography , ionic bonding , site directed spin labeling , spin (aerodynamics) , adsorption , chemical physics , materials science , physics , biochemistry , ion , thermodynamics , aqueous solution , composite material , organic chemistry , membrane
Spin doctoring : Site‐directed spin labeling was used to determine the structure of T4 lysozyme adsorbed on quartz. At high ionic strength significant changes of the backbone fold are limited to the region around the enzymatic cleft. In contrast, at low ionic strength the previously unperturbed parts of the protein interact with the surface. Hydrophobic interactions are thought to play an important role in the partial unfolding at high ionic strength.