THE ENERGY LANDSCAPES AND MOTIONS OF PROTEINS

被引:2725
作者
FRAUENFELDER, H [1 ]
SLIGAR, SG [1 ]
WOLYNES, PG [1 ]
机构
[1] UNIV ILLINOIS, BECKMAN INST, URBANA, IL 61801 USA
关键词
D O I
10.1126/science.1749933
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
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收藏
页码:1598 / 1603
页数:6
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