How the hydrophobic factor drives protein folding

Baldwin Robert L.; Rose George D.

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How the hydrophobic factor drives protein folding

机译：How the hydrophobic factor drives protein folding

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How hydrophobicity (HY) drives protein folding is studied. The 1971 Nozaki-Tanford method of measuring HY is modified to use gases as solutes, not crystals, and this makes the method easy to use. Alkanes are found to be much more hydrophobic than rare gases, and the two different kinds of HY are termed intrinsic (rare gases) and extrinsic (alkanes). The HY values of rare gases are proportional to solvent-accessible surface area (ASA), whereas the HY values of alkanes depend on special hydration shells. Earlier work showed that hydration shells produce the hydration energetics of alkanes. Evidence is given here that the transfer energetics of alkanes to cyclohexane Wolfenden R, Lewis CA, Jr, Yuan Y, Carter CW, Jr (2015) Proc Natl Acad Sci USA 112(24): 74847488 measure the release of these shells. Alkane shells are stabilized importantly by van der Waals interactions between alkane carbon and water oxygen atoms. Thus, rare gases cannot form this type of shell. The very short (approximately picoseconds) lifetime of the van der Waals interaction probably explains why NMR efforts to detect alkane hydration shells have failed. The close similarity between the sizes of the opposing energetics for forming or releasing alkane shells confirms the presence of these shells on alkanes and supports Kauzmann's 1959 mechanism of protein folding. A space-filling model is given for the hydration shells on linear alkanes. The model reproduces the n values of Jorgensen et al. Jorgensen WL, Gao J, Ravimohan C (1985) J Phys Chem 89: 3470-3473 for the number of waters in alkane hydration shells.

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《Proceedings of the National Academy of Sciences of the United States of America.》 |2016年第44期|12462-12466|共5页
作者
Baldwin Robert L.; Rose George D.;
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作者单位

Stanford Univ, Med Ctr, Dept Biochem, Beckman Ctr,Sch Med, Stanford, CA 94305 USA;

Johns Hopkins Univ, Jenkins Dept Biophys, Baltimore, MD 21218 USA;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
protein folding; hydrophobicity; hydrophobic effect; hydration shells; solvent shells;

How the hydrophobic factor drives protein folding

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