EXPOSURE OF TRYPTOPHANYL RESIDUES IN PROTEINS - QUANTITATIVE-DETERMINATION BY FLUORESCENCE QUENCHING STUDIES
EXPOSURE OF TRYPTOPHANYL RESIDUES IN PROTEINS - QUANTITATIVE-DETERMINATION BY FLUORESCENCE QUENCHING STUDIES
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DOI:
10.1021/bi00648a035
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发表时间:
1976-01-01
期刊:
影响因子:
2.9
通讯作者:
GHIRON, CA
中科院分区:
文献类型:
--
作者:
EFTINK, MR;GHIRON, CA
M. R. Eftink and C. A. Ghiron* abstract: Acrylamide is an efficient quencher of trypto-phanyl fluorescence which we report to be very discriminat-ing in sensing the degree of exposure of this residue in pro-teins. The quenching reaction involves physical contact be-tween the quencher and an excited indole ring, and can be kinetically described in terms of a collisional and a static component. The rate constant for the collisional component is a kinetic measure of the exposure of a residue in a pro-tein, and values ranging from 4 X 109 M-1 s~* for the fully exposed tryptophan in the polypeptide, adrenocorticotropin, to< 5 X 108 M-1 s-1 for the buried residue in azurin have