Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin

Molecular and Cellular Biochemistry

Volumn 220, Issue 1-2, 2001, Pages 127-133

  Shroff, N P ^a   Bera, S ^a   Cherian Shaw, M ^a   Abraham, E C ^a  

^a UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

B crystallin; Chaperone activity; Hydrophilic; Hydrophobic

Indexed keywords

ALPHA CRYSTALLIN; AMINO ACID; CHAPERONE; ISOLEUCINE; METHIONINE; THREONINE; VALINE;

ANIMAL TISSUE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CONTROLLED STUDY; CORRELATION FUNCTION; HYDROPHILICITY; HYDROPHOBICITY; MOLECULAR WEIGHT; MUTATION; NONHUMAN; PROTEIN TARGETING; RAT;

ANIMALS; BINDING SITES; BLOTTING, WESTERN; CIRCULAR DICHROISM; CLONING, MOLECULAR; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ISOLEUCINE; METHIONINE; MUTAGENESIS, SITE-DIRECTED; MUTATION; NAPHTHALENESULFONATES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TEMPERATURE; THREONINE; TIME FACTORS; VALINE;

EID: 0034992086     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010834107809     Document Type: Article

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