The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation

Biochemistry

Volumn 51, Issue 24, 2012, Pages 4822-4834

  Entzminger, Kevin C ^a   Chang, Christine ^c   Myhre, Ryan O ^c   McCallum, Katie C ^b   Maynard, Jennifer A ^c  

^a The University of Texas at Austin   (United States)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^c The University of Texas at Austin   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PROTEINS; AQUEOUS ENVIRONMENT; BIOPHYSICAL CHARACTERISTICS; CO-EXPRESSION; FOLDING INTERMEDIATES; FOLDING RATES; IN-VITRO; IN-VIVO; OUTER MEMBRANE PROTEIN; PERIPLASM; PERIPLASMIC PROTEINS; RECOMBINANT PROTEIN EXPRESSION; REFOLDING; SINGLE-CHAIN ANTIBODIES; SOLUBLE PROTEINS; T-CELL RECEPTORS; VIRULENCE FACTORS;

CELL MEMBRANES; MACHINERY; PROTEIN FOLDING; UREA;

RECOMBINANT PROTEINS;

BACTERIAL PROTEIN; CHAPERONE; PERIPLASMIC PROTEIN; SEVENTEEN KILODALTON PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; UREA;

ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; HYPOTHESIS; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SENSITIVITY ANALYSIS;

ANIMALS; DNA-BINDING PROTEINS; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MURAMIDASE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN REFOLDING; PROTEIN STRUCTURE, QUATERNARY; SINGLE-CHAIN ANTIBODIES; SOLUBILITY; UREA;

EID: 84862557282     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300412y     Document Type: Article

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