A. Joshua Wand

TL;DR: It is found that the change in internal dynamics of the protein calmodulin varies significantly on binding a variety of target domains, indicating that changes in protein conformational entropy can contribute significantly to the free energy of protein–ligand association.

TL;DR: This review seeks to provide a compact but reasonably complete description of the theoretical and technical foundation for solution NMR relaxation methods that are currently being brought to bear on fast subnanosecond protein side chain dynamics and to present a summary of current findings and their possible significance.

TL;DR: These data provide a microscopic view of the residual entropy of aprotein in two functional states and suggest extensive enthalpy/entropy exchange during the formation of a protein–protein interface.

TL;DR: A survey of the temperature dependence of the fast dynamics of methyl-bearing side chains in a calmodulin–peptide complex using site-specific deuterium NMR relaxation methods indicates a heterogeneous distribution of residual entropy and reveals the microscopic origins of heat capacity in proteins.

TL;DR: An “entropy meter” is calibrated employing an experimental dynamical proxy based on NMR relaxation and it is shown that changes in the conformational entropy of calmodulin are a significant component of the energetics of binding and the distribution of motion at the interface between the target domain and cal modulin are surprisingly non-complementary.