Thermodynamic insights into proteins from NMR spin relaxation studies

NMR spin relaxation measurements of picosecond to nanosecond timescale back bone and sidechain fluctuations of protein molecules, and subsequent entrop ic interpretation yield interesting, but sometimes counterintuitive, insigh ts into proteins. The stabilities of proteins and protein interactions are achieved through enthalpy-entropy compensation, which is partitioned betwee n the backbone and sidechains depending on the nature of the system.