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CiteWeb id: 19910000231

CiteWeb score: 2668

DOI: 10.1126/science.1749933

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.

The publication "The energy landscapes and motions of proteins." is placed in the Top 10000 of the best publications in CiteWeb. Also in the category Chemistry it is included to the Top 1000. Additionally, the publicaiton "The energy landscapes and motions of proteins." is placed in the Top 1000 among other scientific works published in 1991.
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