Proteins are dynamic, flexible polymers, Thermally driven, stochastic motions, modulate all aspects of their structure. Bonds vibrate, side chains rotate, surface loops wiggle, domains flex about their connecting links, and the entire structure 'breathes' by fluctuating about the most stable conformation. This internal flexibility provides a dynamic foundation for biological functions and for functionalities in foods ranging from enzyme catalysis to gelation. This review describes the various physical modes and timescales of internal protein dynamics; including their physical origins and the factors that modulate them, and summarizes the physical techniques used to measure molecular dynamics in the skeletal muscle protein, myosin.
All Science Journal Classification (ASJC) codes
- Food Science