A PROTEIN DISSECTION STUDY OF A MOLTEN GLOBULE

被引：200

作者：

PENG, ZY ^{[1
]}

KIM, PS ^{[1
]}

机构：

[1] MIT,WHITEHEAD INST BIOMED RES,HOWARD HUGHES MED INST,DEPT BIOL,CAMBRIDGE,MA 02142

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 08期

关键词：

D O I：

10.1021/bi00174a021

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：

Proteins have many distinct tertiary folds (Richardson, J. S. (1981) Adv. Prot. Chem. 34, 167-339). The term tertiary fold refers to the spatial organization of secondary structure elements (alpha-helices and beta-strands). It is not known when, in the process of protein folding, a native tertiary fold emerges. Here, we show that the helical domain of human alpha-lactalbumin, in isolation, forms a molten globule with the same overall tertiary fold as that found in intact alpha-lactalbumin. Formation of this nativelike fold does not require extensive, specific side-chain packing. Our results suggest that much of the information transfer from one-dimension to three-dimensions has occurred at the molten globule stage of protein folding.

引用

页码：2136 / 2141

页数：6

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