Topological Switching between an α-β parallel protein and a remarkably helical molten globule

Journal of the American Chemical Society

Volumn 131, Issue 23, 2009, Pages 8290-8295

  Nabuurs, Sanne M ^a   Westphal, Adrie H ^a   Aan Den Toorn, Marije ^a   Lindhoud, Simon ^a   Van Mierlo, Carlo P M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; FLAVODOXIN; FOLDED PROTEINS; MOLTEN GLOBULE; NATIVE PROTEINS; NON-NATIVE SPECIES; PROTEIN STRUCTURES; SECONDARY STRUCTURES; SIDE-CHAIN; SPECTROSCOPIC CHARACTERIZATION;

AMINES; AMINO ACIDS; ORGANIC ACIDS;

PROTEIN FOLDING;

ALPHA BETA PARALLEL PROTEIN; AMINO ACID; APOFLAVODOXIN; FLAVODOXIN; GLOBULAR PROTEIN; MOLTEN GLOBULE; PHENYLALANINE; POLYPEPTIDE; PROTEIN; TYROSINE; UNCLASSIFIED DRUG; APOPROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; AZOTOBACTER VINELANDII; BETA SHEET; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; SPECTROSCOPY; CHEMICAL MODEL; CHEMISTRY; GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

APOPROTEINS; CONSERVED SEQUENCE; FLAVODOXIN; MODELS, CHEMICAL; PHENYLALANINE; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; TYROSINE;

EID: 67650546929     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9014309     Document Type: Article

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