两种不含色氨酸的蛋白质（组蛋白H1和H5）的酪氨酸荧光

Tyrosine fluorescence of two tryptophan-free proteins: histones H1 and H5.

作者信息

Giancotti V, Fonda M, Crane-Robinson C

出版信息

Biophys Chem. 1977 Apr;6(3):379-83. doi: 10.1016/0301-4622(77)85019-9.

Abstract

The fluorescence intensity of the single tyrosine residue in histone H1 increases from RTYR = 0.3 to RTYR = 1.3 as the protein undergoes a conformational change from the random coil state to a folded form. Enhanced fluorescence in the folded state has not been observed before in ap protein. Histone H5 shows no change in fluorescence intensity on folding. This is interpreted as a result of compensation between enhanced and reduced fluorescence in the three tyrosine residues.

摘要

随着蛋白质从无规卷曲状态转变为折叠形式，组蛋白H1中单个酪氨酸残基的荧光强度从RTYR = 0.3增加到RTYR = 1.3。此前在脱辅基蛋白中未观察到折叠状态下荧光增强的情况。组蛋白H5在折叠时荧光强度没有变化。这被解释为三个酪氨酸残基中荧光增强和减弱之间相互补偿的结果。