Molecular dynamics simulations of Hydrogenobacter thermophilus cytochrome c552: Comparisons of the wild-type protein, a b-type variant, and the apo state

Proteins: Structure, Function and Genetics

Volumn 65, Issue 3, 2006, Pages 702-711

  Smith, Lorna J ^a   Davies, Robert J ^a   Van Gunsteren, Wilfred F ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b ETH ZURICH   (Switzerland)

Author keywords

Amyloid fibril; c type cytochrome; GROMOS96; Heme; MD simulation; NMR data; Protein dynamics

Indexed keywords

ALANINE; AMYLOID; CYSTEINE; CYTOCHROME C; CYTOCHROME C552; GLYCINE; HEME; PROPIONIC ACID; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; BINDING SITE; CONFORMATIONAL TRANSITION; COVALENT BOND; HYDROGEN BOND; HYDROGENOBACTER THERMOPHILUS; METHANOBACTERIUM; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN VARIANT; SIMULATION; WILD TYPE;

ALANINE; APOPROTEINS; BACTERIAL PROTEINS; BINDING SITES; CYSTEINE; CYTOCHROME C GROUP; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY;

HYDROGENOBACTER THERMOPHILUS;

EID: 33750045162     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21141     Document Type: Article

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