NATURAL POLYPEPTIDES IN LEFT-HANDED HELICAL CONFORMATION - A CIRCULAR-DICHROISM STUDY OF THE LINKER HISTONES C-TERMINAL FRAGMENTS AND BETA-ENDORPHIN

被引：30

作者：

MAKAROV, AA ^{[1
]}

LOBACHOV, VM ^{[1
]}

ADZHUBEI, IA ^{[1
]}

ESIPOVA, NG ^{[1
]}

机构：

[1] MV LOMONOSOV STATE UNIV,FAC BIOL,DEPT MOLEC BIOL,MOSCOW 119899,USSR

来源：

FEBS LETTERS | 1992年 / 306卷 / 01期

关键词：

LINKER HISTONE; BETA-ENDORPHIN; CIRCULAR DICHROISM; POLY-L-PROLINE-II CONFORMATION; NONCOOPERATIVE MELTING;

D O I：

10.1016/0014-5793(92)80838-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Circular dichroism has been used to investigate the histone H1 and H5 C-terminal fragments and beta-endorphin conformation. It has been shown that in aqueous solution these polypeptides preferably adopt the left-handed helical conformation of the poly-L-proline II type. A break in the linear temperature dependence of the CD value was found in the temperature interval between 50 and 55-degrees-C. It was proposed to be due to non-cooperative disordering of the conformation caused by the destruction of the hydration shell.

引用

页码：63 / 65

页数：3

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