Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of α-β parallel protein flavodoxin

Journal of Biological Chemistry

Volumn 285, Issue 6, 2010, Pages 4165-4172

  Nabuurs, Sanne M ^a   Van Mierlo, Carlo P M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CONTEXT DEPENDENT; DENATURING CONDITIONS; DETRIMENTAL EFFECTS; FLAVODOXIN; FOLDED PROTEINS; FOLDING INTERMEDIATES; HYDROGEN/DEUTERIUM EXCHANGE; HYDROPHOBIC GROUPS; MOLTEN GLOBULE; NATIVE STATE; NMR SPECTROSCOPY; NON-NATIVE SPECIES; PROTEIN MOLECULES; RESIDUE LEVEL; SECONDARY STRUCTURES; SIDE-CHAIN;

PROTEIN FOLDING;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

DEUTERIUM; FLAVODOXIN; HYDROGEN; LEUCINE; PHENYLALANINE; TYROSINE; VALINE; BACTERIAL PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; AZOTOBACTER VINELANDII; BETA SHEET; CONTROLLED STUDY; DENATURATION; DEUTERIUM HYDROGEN EXCHANGE; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; ALGORITHM; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

AZOTOBACTER VINELANDII;

ALGORITHMS; AMINO ACID SUBSTITUTION; AZOTOBACTER VINELANDII; BACTERIAL PROTEINS; DEUTERIUM EXCHANGE MEASUREMENT; FLAVODOXIN; HYDROPHOBICITY; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TYROSINE;

EID: 77950490437     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.087932     Document Type: Article

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