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Adventures in Experimental Protein Biophysics: Filling the Gaps in Our Knowledge of How Proteins Work

The vast majority of the work in living systems is executed by proteins, so they are a central focus of many biophysical investigations. It is well known that protein structures and protein functions are dictated by thermodynamics, and while the enthalpic contributions to protein structure-function relationships are well understood, the entropic contributions remain largely a mystery. Recent studies using nuclear magnetic resonance (NMR) have shed exciting new light on the entropic nature of proteins and have revealed a likely functional role for the internal entropy of proteins and for the entropy of the water that solvates them. These recent findings and their implications for understanding (and manipulating!) protein function will be discussed. New studies using fluorescence techniques to understand anomalous diffusion in cells will also be summarized.