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Volumn 41, Issue 1, 2002, Pages 297-305
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The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin
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Author keywords
[No Author keywords available]
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Indexed keywords
MUTANTS;
ELECTROPHORESIS;
FLUORESCENCE;
GEL PERMEATION CHROMATOGRAPHY;
GELS;
MUTAGENESIS;
BIOCHEMISTRY;
ALPHA B CRYSTALLIN;
ALPHA CRYSTALLIN;
CHAPERONE;
ISOPROTEIN;
MUTANT PROTEIN;
PROTEIN SUBUNIT;
UNCLASSIFIED DRUG;
1-ANILINO-8-NAPHTHALENESULFONATE;
8 ANILINO 1 NAPHTHALENESULFONIC ACID;
CRYSTALLIN;
FLUORESCENT DYE;
ARTICLE;
BINDING AFFINITY;
CIRCULAR DICHROISM;
CONGENITAL CATARACT;
FLUORESCENCE SPECTROSCOPY;
GENE MUTATION;
HEAT SENSITIVITY;
HYDROPHOBICITY;
MOLECULAR WEIGHT;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN BINDING;
PROTEIN MODIFICATION;
ANIMAL;
BINDING SITE;
COMPARATIVE STUDY;
DRUG EFFECT;
ENZYMOLOGY;
ESCHERICHIA COLI;
KINETICS;
METABOLISM;
MUTATION;
PROTEIN CONFORMATION;
RAT;
TEMPERATURE;
TIME;
ANILINO NAPHTHALENESULFONATES;
ANIMALS;
BINDING SITES;
CIRCULAR DICHROISM;
CRYSTALLINS;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ESCHERICHIA COLI;
FLUORESCENT DYES;
KINETICS;
MOLECULAR CHAPERONES;
MUTATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN SUBUNITS;
RATS;
TEMPERATURE;
TIME FACTORS;
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EID: 0037039153
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011010v Document Type: Article |
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Times cited : (52)
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References (36)
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