NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold

Biochemistry

Volumn 43, Issue 47, 2004, Pages 14971-14978

  Paquet, Françoise ^a   Culard, Françoise ^a   Barbault, Florent ^b   Maurizot, Jean Claude ^a   Lancelot, Gérard ^a  

^a CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

^b UNIVERSITÉ PARIS DIDEROT   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; CROSSLINKING; DNA; HYDROPHILICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; SOLVENTS;

ARCHAEBACTERIAL CHROMOSOMAL PROTEIN; DNA-BINDING PROTEINS; METHANOGEN CHROMOSOMAL PROTEIN 1 (MC1); THREE-DIMENSIONAL STRUCTURES;

CHROMOSOMES;

BACTERIAL PROTEIN; CHROMOSOMAL PROTEIN MC1; CHROMOSOME PROTEIN; HIGH MOBILITY GROUP B PROTEIN; HU PROTEIN; PROLINE; PROTEIN P68; PROTEIN P76; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARCHAEBACTERIUM; ARTICLE; DNA BINDING; METHANOSARCINA; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; AMINO ACIDS, ACIDIC; AMINO ACIDS, BASIC; ARCHAEA; ARCHAEAL PROTEINS; BINDING SITES; BUFFERS; CROSS-LINKING REAGENTS; DNA-BINDING PROTEINS; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; METHANOSARCINA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTONS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; SPECTRUM ANALYSIS, RAMAN; TEMPERATURE; TRYPTOPHAN;

ARCHAEA; BACTERIA (MICROORGANISMS); METHANOSARCINA; METHANOSARCINA SP.;

EID: 9744245199     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048382z     Document Type: Article

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