IDENTIFICATION BY H-1-NMR SPECTROSCOPY OF FLEXIBLE C-TERMINAL EXTENSIONS IN BOVINE LENS ALPHA-CRYSTALLIN

被引：134

作者：

CARVER, JA ^{[1
]}

AQUILINA, JA ^{[1
]}

TRUSCOTT, RJW ^{[1
]}

RALSTON, GB ^{[1
]}

机构：

[1] UNIV SYDNEY,DEPT BIOCHEM,SYDNEY,NSW 2006,AUSTRALIA

来源：

FEBS LETTERS | 1992年 / 311卷 / 02期

关键词：

LENS; CRYSTALLIN; NMR; CONFORMATION; AGGREGATION;

D O I：

10.1016/0014-5793(92)81386-Z

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：

Two-dimensional H-1 NMR spectroscopy of bovine eye lens alpha-crystallin and its isolated alpha(A) and alpha(B) subunits reveals that these aggregates have short and very flexible C-terminal extensions of eight (alpha(A)) and ten (alpha(B)) amino acids which adopt little preferred conformation in solution. Total alpha-crystallin forms a tighter aggregate than the isolated alpha(A) and alpha(B) subunit aggregates. Our results are consistent with a micelle model for alpha-crystallin quaternary structure. The presence of terminal extensions is a general feature of those crystallins, alpha and beta, which form aggregates.

引用

页码：143 / 149

页数：7

共 30 条

[1] STRUCTURAL HOMOLOGY OF LENS CRYSTALLINS - A METHOD TO DETECT PROTEIN STRUCTURAL HOMOLOGY FROM PRIMARY SEQUENCES [J].