TY - JOUR
T1 - Molecular dynamics of food proteins
T2 - experimental techniques and observations
AU - Ludescher, Richard D.
PY - 1990/7
Y1 - 1990/7
N2 - 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.
AB - 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.
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U2 - 10.1016/0924-2244(90)90112-C
DO - 10.1016/0924-2244(90)90112-C
M3 - Review article
AN - SCOPUS:0006725329
VL - 1
SP - 145
EP - 149
JO - Trends in Food Science and Technology
JF - Trends in Food Science and Technology
SN - 0924-2244
IS - C
ER -