NMR structures and orientation of the fourth transmembrane domain of the rat divalent metal transporter (DMT1) with G185D mutation in SDS micelles

Biopolymers

Volumn 77, Issue 4, 2005, Pages 173-183

  Li, Hongyan ^a   Li, Fei ^a   Kwan, Miufan ^a   He, Qing Yu ^a   Sun, Hongzhe ^a  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

CD, DMT1; Micelle; NMR; Transmembrane peptide

Indexed keywords

FOURTH TRANSMEMBRANE DOMAIN (TM4); MEMBRANE MIMETIC ENVIRONMENTS; MEMBRANE-MIMETIC ENVIRONMENTS; SYNTHETIC PEPTIDES;

ANNEALING; DISEASES; HYDROPHILICITY; LIVING SYSTEMS STUDIES; MICELLES; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS; PROTEINS; RESONANCE; STRUCTURE (COMPOSITION);

BIOLOGICAL MEMBRANES;

ASPARTIC ACID; DODECYL SULFATE SODIUM; GLYCINE; IRON; MANGANESE; METAL ION; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 1; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; SYNTHETIC PEPTIDE; THREONINE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; GENE MUTATION; GENETIC CONSERVATION; HYDROPHILICITY; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PERMEABILITY; PH; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RAT; SIMULATION; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ACID; CATION TRANSPORT PROTEINS; CIRCULAR DICHROISM; GLYCINE; MICELLES; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RATS; SODIUM DODECYL SULFATE;

EID: 15944397322     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.20204     Document Type: Article

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