UV resonance Raman investigations of peptide and protein structure and dynamics.
UV resonance Raman investigations of peptide and protein structure and dynamics.
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DOI:
10.1021/cr200198a
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发表时间:
2012-05-09
期刊:
影响因子:
62.1
通讯作者:
Lednev, Igor K.
中科院分区:
文献类型:
--
作者:
Oladepo, Sulayman A.;Xiong, Kan;Hong, Zhenmin;Asher, Sanford A.;Handen, Joseph;Lednev, Igor K.
1.1. Protein Folding Problem An understanding of the mechanism (s) of protein folding, whereby the ribosome synthesized biopolymer folds into its native protein, is arguably one of the most important unsolved problems in biology. 1À7 The primary sequence of many or most proteins encodes both the native structure and the folding mechanism pathway to the native structure. 8À10 Over the last 50 years numerous groups have examined the mechanisms of protein folding, with a major objective being to develop methods to predict the native conformation from the primary protein sequence. An understanding of the encoded protein folding “rules” would dramatically speed insight into protein structure and function; this knowledge would result in the first principles design of drugs to treat human diseases, many of which result from protein mutations and/or from protein misfolding. A vast theoretical and experimental literature exists on protein folding. A number of mechanisms have been proposed that differ in the order of folding events. For example, the framework model11 and the diffusion-collision model12 propose that the initial step in folding involves formation of native-like secondary structural units, whereas the hydrophobic collapse model13, 14 and the nucleation-condensation model14 suggest that hydrophobic or nucleating domains fold first, and that these structures drive the subsequent formation of secondary structure. Recent energy landscape models4, 15À24 propose the occurrence of funnel-shaped folding energy landscapes, where the native state is accessed via a strategically sloped energy landscape that funnels myriads of partially folded conformations toward the native folded state. 4, 25, 26
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影响因子:
13.8
作者:
Baldwin, RL;Rose, GD
通讯作者:
Rose, GD
影响因子:
7.4
作者:
ASHER, SA
通讯作者:
ASHER, SA
影响因子:
3.3
作者:
Balakrishnan, Gurusamy;Hu, Ying;Spiro, Thomas G.
通讯作者:
Spiro, Thomas G.
影响因子:
13.8
作者:
Baldwin, RL;Rose, GD
通讯作者:
Rose, GD
DOI:
10.1107/s0567740882004075
发表时间:
1982-01-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE
影响因子:
--
作者:
ARTYMIUK, PJ;BLAKE, CCF;WILSON, KS
通讯作者:
WILSON, KS