PROSTATIC INHIBIN HAS A PREDOMINANTLY ANTI-PARALLEL BETA-SHEET STRUCTURE

被引：0

作者：

CHARY, KVR ^{[1
]}

RASTOGI, VK ^{[1
]}

GOVIL, G ^{[1
]}

GARDE, SV ^{[1
]}

SHETH, AR ^{[1
]}

机构：

[1] INST RES REPROD,BOMBAY 400012,INDIA

来源：

CURRENT SCIENCE | 1993年 / 65卷 / 10期

关键词：

D O I：

暂无

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Prostatic inhibin (94 amino acid residues, M(r) = 10,540) is a protein isolated from the human and animal prostate glands. Three-dimensional structure of this cysteine-rich (10/94) protein has been studied by NMR spectroscopy. Preliminary investigations provide valuable information on the secondary structure of this protein. It is found to acquire a predominantly anti-parallel beta-sheet structure and possibly the molecule is locked into several such sheets through disulphide linkages.

引用

页码：786 / 789

页数：4

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