Structure and Function of the Middle Domain of ClpB from Escherichia coli

Biochemistry

Volumn 42, Issue 48, 2003, Pages 14242-14248

  Kedzierska, Sabina ^b   Akoev, Vladimir ^a   Barnett, Micheal E ^a   Zolkiewski, Michal ^a  

^a KANSAS STATE UNIVERSITY   (United States)

^b UNIVERSITY OF GDA SK   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; ENZYMES; ESCHERICHIA COLI; OLIGOMERS; THERMODYNAMICS;

HELICAL STRUCTURES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CHAPERONE; CLPA PROTEIN; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN F84.1, E COLI; HEAT-SHOCK PROTEIN F84.1, E COLI; MONOMER; PEPTIDASE; PEPTIDE FRAGMENT; PROTEIN CLPB; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN GRPE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CHEMISTRY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; GENETICS; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; NONHUMAN; NUCLEOTIDE REPEAT; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT; SEDIMENTATION; SEQUENCE HOMOLOGY; SOLUTION AND SOLUBILITY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REPETITIVE SEQUENCES, AMINO ACID; SEQUENCE DELETION; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP; ULTRACENTRIFUGATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0344629876     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035573d     Document Type: Article

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