Article ID Journal Published Year Pages File Type
5371392 Biophysical Chemistry 2011 7 Pages PDF
Abstract
► LC8 partners are grouped as those whose binding is enthalpically favored and those whose binding is entropically favored. ► Changes in LC8 flexibility upon binding are peptide dependent. ► Binding of some peptides rigidifies the binding groove, while others do not change the dynamics of the free protein. ► The change in total entropy measured by ITC correlates with the NMR-determined changes in LC8 backbone heterogeneity. ► The dynamical properties retained by the peptide and by the LC8 pocket compensate for lack of crucial conserved interactions.
Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
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