Local and coupled thermodynamic stability of the two-domain and bifunctional enzyme SlyD from Escherichia coli

Biochemistry

Volumn 50, Issue 34, 2011, Pages 7321-7329

  Haupt, Caroline ^a   Weininger, Ulrich ^a,b   Kovermann, Michael ^a   Balbach, Jochen ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

2D-NMR SPECTROSCOPY; AMIDE PROTON; BIFUNCTIONAL ENZYMES; BIOPHYSICAL TECHNIQUES; CHAPERONE ACTIVITY; CHAPERONE FUNCTIONS; COOPERATIVITY; DENATURING CONDITIONS; DIVALENT CATION; INTERNAL FLUCTUATION; LOCAL STABILITY; PEPTIDYL-PROLYL ISOMERASE; PROTEIN SUBSTRATE; TWO DOMAINS;

AMIDES; ENZYMES; ESCHERICHIA COLI; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; PROTEINS; THERMODYNAMICS; UREA;

THERMODYNAMIC STABILITY;

BACTERIAL ENZYME; METALLOCHAPERONE; NICKEL; PEPTIDYLPROLYL ISOMERASE; PROTEIN SLYD; UNCLASSIFIED DRUG; UREA;

ARTICLE; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; THERMODYNAMICS;

AMIDES; DEUTERIUM EXCHANGE MEASUREMENT; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; PEPTIDYLPROLYL ISOMERASE; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; PROTONS; THERMODYNAMICS; UREA;

ESCHERICHIA COLI;

EID: 80051984524     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2000627     Document Type: Article

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