Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5371392 | Biophysical Chemistry | 2011 | 7 Pages |
Abstract
⺠LC8 partners are grouped as those whose binding is enthalpically favored and those whose binding is entropically favored. ⺠Changes in LC8 flexibility upon binding are peptide dependent. ⺠Binding of some peptides rigidifies the binding groove, while others do not change the dynamics of the free protein. ⺠The change in total entropy measured by ITC correlates with the NMR-determined changes in LC8 backbone heterogeneity. ⺠The dynamical properties retained by the peptide and by the LC8 pocket compensate for lack of crucial conserved interactions.
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Chemistry
Physical and Theoretical Chemistry
Authors
Afua Nyarko, Justin Hall, Andrea Hall, Michael Hare, Joachim Kremerskothen, Elisar Barbar,