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Volumn 363, Issue 2, 2002, Pages 329-334
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The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein hsp16.3 occurs via a stepwise mechanism
a a a a a |
Author keywords
Electrophoresis; Oligomeric protein; Reassembling; Urea denaturing; Urea gradient PAGE
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Indexed keywords
BACTERIA;
DIALYSIS;
OLIGOMERS;
PROTEINS;
UREA;
OLIGOMERIC PROTEINS;
BIOCHEMISTRY;
HEAT SHOCK PROTEIN;
HEAT SHOCK PROTEIN 16.3;
UNCLASSIFIED DRUG;
UREA;
ARTICLE;
ELECTROPHORESIS;
GENE OVEREXPRESSION;
MYCOBACTERIUM TUBERCULOSIS;
NONHUMAN;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
PROTEIN DENATURATION;
PROTEIN FAMILY;
PROTEIN FOLDING;
PROTEIN PURIFICATION;
PROTEIN QUATERNARY STRUCTURE;
BACTERIAL PROTEINS;
CHAPERONINS;
MODELS, MOLECULAR;
MYCOBACTERIUM TUBERCULOSIS;
POINT MUTATION;
PROTEIN DENATURATION;
PROTEIN RENATURATION;
PROTEIN STRUCTURE, QUATERNARY;
UREA;
MYCOBACTERIUM;
MYCOBACTERIUM TUBERCULOSIS;
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EID: 0037090621
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3630329 Document Type: Article |
Times cited : (10)
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References (22)
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