Susceptibility of Different Proteins to Flow-Induced Conformational Changes Monitored with Raman Spectroscopy

被引：33

作者：

Ashton, Lorna ^{[1
,2
]}

Dusting, Jonathan ^{[3
]}

Imomoh, Eboshogwe ^{[3
]}

Balabani, Stavroula ^{[3
]}

Blanch, Ewan W. ^{[1
,2
]}

机构：

[1] Univ Manchester, Manchester Interdisciplinary Bioctr, Manchester, Lancs, England

[2] Univ Manchester, Fac Life Sci, Manchester, Lancs, England

[3] Kings Coll London, Div Engn, Expt & Computat Lab Anal Turbulence, London WC2R 2LS, England

来源：

BIOPHYSICAL JOURNAL | 2010年 / 98卷 / 04期

基金：

英国工程与自然科学研究理事会;

关键词：

BETA-LACTOGLOBULIN; STRUCTURAL-CHARACTERIZATION; SECONDARY STRUCTURE; CONCANAVALIN-A; CASEIN; PHOSPHORYLATION; TRANSITION; FETUIN; STABILITY; MECHANICS;

D O I：

10.1016/j.bpj.2009.10.010

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

By directly monitoring stirred protein solutions with Raman spectroscopy, the reversible unfolding of proteins caused by fluid shear is examined for several natural proteins with varying structural properties and molecular weight. While complete denaturation is not observed. a wide range of spectral variances occur for the different proteins, indicating subtle conformational changes that appear to be protein-specific A number of significant overall trends are apparent from the study For globular proteins, the overall extent of spectral variance increases with protein size and the proportion of beta-structure For two less structured proteins, fetuin and a-casein. the observed changes are of relatively low magnitude, despite the greater molecular structural mobility of these proteins This implies that other protein-specific factors, such as posttranslational modifications, may also be significant Individual band changes occurring in the spectral profiles of each individual protein are also discussed in detail

引用

页码：707 / 714

页数：8

共 46 条

[1] Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains [J].