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A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin

Date

Authors

Treweek, Teresa

Rekas, Agata

Walker, Mark J.

Carver, John

Publisher

Academic Press

Abstract

The principal lens proteins αA- and αB-crystallin are members of the small heat-shock protein (sHsp) family of molecular chaperone proteins. Via their chaperone action, αA- and αB-crystallin play an important role in maintaining lens transparency by p

Keywords

Keywords: alpha crystallin; alpha lactalbumin; beta crystallin; chaperone; article; carboxy terminal sequence; heteronuclear single quantum coherence; lens; mutant; nitrogen nuclear magnetic resonance; nuclear magnetic resonance spectroscopy; nuclear Overhauser eff C-terminal extension; Molecular chaperone; NMR Spectroscopy; Site directed mutagenesis; Small heat-shock protein

URI

http://hdl.handle.net/1885/63298

Collections

ANU Research Publications

Source

Experimental Eye Research

Type

Journal article

DOI

10.1016/j.exer.2010.08.015

Restricted until

2037-12-31

Downloads

File

Description

01_Treweek_A_quantitative_NMR_2010.pdf (567.21 KB)