Cross-β Spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fiber diffraction measurements

Biochemistry

Volumn 48, Issue 14, 2009, Pages 3089-3099

  Madine, Jillian ^a   Copland, Alastair ^b   Serpell, Louise C ^b   Middleton, David A ^a  

^a UNIVERSITY OF LIVERPOOL   (United Kingdom)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACID POLYPEPTIDES; ATOMIC SITES; DEGREE OF ORDERS; EXPERIMENTAL DATUM; MODEL PEPTIDES; MOLECULAR ARCHITECTURES; MOLECULAR MODELS; PATHOLOGICAL DISORDERS; ROTATIONAL RESONANCES; SOLID-STATE NMR; SOLID-STATE NUCLEAR MAGNETIC RESONANCES; STRUCTURAL STUDIES; X-RAY FIBER DIFFRACTIONS;

AMINO ACIDS; DIFFRACTION; GLYCOPROTEINS; HOLOGRAPHIC INTERFEROMETRY; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS; PEPTIDES; POLYPEPTIDES; RESONANCE;

AMINES;

AMINO ACID; AMYLOID; ASPARAGINYLPHENYLALANYLGLYCYLSERYLVALYLGLUTAMINYLPHENYLALANYLVALINE; CARBON 13; PEPTIDE DERIVATIVE; POLYPEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; BETA SHEET; CHEMICAL STRUCTURE; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR INTERACTION; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; SOLID STATE; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMYLOID; ANTIGENS, SURFACE; CARBON ISOTOPES; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MILK PROTEINS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; X-RAY DIFFRACTION;

EID: 65249169320     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802164e     Document Type: Article

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