Partially folded structure of monomeric bovine beta-lactoglobulin

被引：106

作者：

Molinari, H

Ragona, L

Varani, L

Musco, G

Consonni, R

Zetta, L

Monaco, HL

机构：

[1] UNIV VERONA,FAC SCI,IST POLICATTEDRA,I-37100 VERONA,ITALY

[2] EMBL,HEIDELBERG,GERMANY

[3] UNIV PAVIA,DIPARTIMENTO GENET,I-27100 PAVIA,ITALY

来源：

FEBS LETTERS | 1996年 / 381卷 / 03期

关键词：

locally unfolded structure; beta-lactoglobulin; CD; NMR;

D O I：

10.1016/0014-5793(96)00100-7

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：

Bovine beta-LG (beta-lactoglobulin) has been studied under a variety of solution conditions by one- and two-dimensional NMR spectroscopy. At highly acidic pH (pH = 2) and low ionic strength the protein is present in a monomeric form, exhibiting a highly structured beta-sheet core and less ordered regions as evidenced by both CD data and the NOESY spectra. Marginal protection was observed for most of the amide protons as a result of high conformational mobility. This structural state of beta-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.

引用

页码：237 / 243

页数：7

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