Journal
BIOPHYSICAL JOURNAL
Volume 91, Issue 6, Pages 2055-2062Publisher
BIOPHYSICAL SOCIETY
DOI: 10.1529/biophysj.106.082180
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It is now recognized that internal global protein dynamics play an important role in the allosteric function of many proteins. Alterations of protein. exibility on effector binding affect the entropic cost of binding at a distant site. We present a coarse-grained model for a potential amplification of such entropic allostery due to coupling of fast, localized modes to the slow, global modes. We show how such coupling can give rise to large compensating entropic and enthalpic terms. The model corresponds to the pattern of calorimetry and NMR data from experiments on the Met repressor.
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