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Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity

Date

Authors

Morris, Amie

Treweek, Teresa

Aquilina, John Andrew

Carver, John

Walker, Mark

Publisher

Blackwell Publishing Ltd

Abstract

Small heat shock proteins (sHsps) are intracellular molecular chaperones that prevent the aggregation and precipitation of partially folded and destabilized proteins. sHsps comprise an evolutionarily conserved region of 80-100 amino acids, denoted the α-

Keywords

Keywords: alanine; glutamic acid; heat shock protein 25; tryptophan; article; hydrophobicity; mutant; nonhuman; priority journal; protein function; protein secondary structure; protein structure; thermostability; Amino Acid Substitution; Amino Acids; Anilino Naphth C-terminal extension; Hsp25; Molecular chaperone; Protein aggregation; Small heat shock protein

URI

http://hdl.handle.net/1885/63172

Collections

ANU Research Publications

Source

The FEBS Journal

Type

Journal article

DOI

10.1111/j.1742-4658.2008.06719.x

Restricted until

2037-12-31

Downloads

File

Description

01_Morris_Glutamic_acid_residues_in_the_2008.pdf (617.41 KB)