THE ROLE OF SOLVENT VISCOSITY IN THE DYNAMICS OF PROTEIN CONFORMATIONAL-CHANGES

被引：508

作者：

ANSARI, A ^{[1
]}

JONES, CM ^{[1
]}

HENRY, ER ^{[1
]}

HOFRICHTER, J ^{[1
]}

EATON, WA ^{[1
]}

机构：

[1] NIDDKD,CHEM PHYS LAB,BLDG 2,BETHESDA,MD 20892

来源：

SCIENCE | 1992年 / 256卷 / 5065期

关键词：

D O I：

10.1126/science.1615323

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：

Nanosecond lasers were used to measure the rate of conformational changes ir myoglobin after ligand dissociation at ambient temperatures. At low solvent viscosities the rate is independent of viscosity, but at high viscosities it depends on approximately the inverse first power of the viscosity. Kramers theory for unimolecular rate processes can be used to explain this result if the friction term is modified to include protein as well as solvent friction. The theory and experiment suggest that the dominant factor in markedly reducing the rate of conformational changes in myoglobin at low temperatures (<200 K) is the very high viscosity (>10(7) centipoise) of the glycerol-water solvent. That is, at low temperatures conformational substates may not be "frozen" so much as "stuck."

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页码：1796 / 1798

页数：3

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