Dynamics of intramolecular contact formation in polypeptides: Distance dependence of quenching rates in a room-temperature glass

被引：60

作者：

Lapidus, LJ ^{[1
]}

Eaton, WA ^{[1
]}

Hofrichter, J ^{[1
]}

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

来源：

PHYSICAL REVIEW LETTERS | 2001年 / 87卷 / 25期

关键词：

D O I：

10.1103/PhysRevLett.87.258101

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

Quenching of the triplet state of tryptophan by cysteine is an important new tool for measuring the rate of forming a specific contact between amino acids in a polypeptide chain. To determine the length scale associated with this contact, tryptophan was embedded in a room-temperature glass containing a high concentration of cysteine. The decay of the triplet population is extended in time, consistent with a rate coefficient that decreases exponentially with distance. Solving the diffusion equation with this distant-dependent rate reproduces the observed bimolecular rates in water and shows that quenching at low viscosities takes place less than or similar to1 Angstrom from van der Waals contact between the tryptophan and cysteine.

引用

页码：258101 / 1

页数：4

共 33 条

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