Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin

Journal of Peptide Science

Volumn 18, Issue 1, 2012, Pages 65-72

  Davies, Hannah A ^a   Madine, Jillian ^a   Middleton, David A ^a  

^a UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

Aortic medial amyloid; Dynamics; Electron microscopy; Structure

Indexed keywords

AMYLOID; MEDIN; PEPTIDE FRAGMENT; POLYPEPTIDE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; FIBER; FLUORESCENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; AMYLOIDOSIS; ANTIGENS, SURFACE; AORTA; BIOLOGICAL MARKERS; DIABETES MELLITUS, TYPE 2; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ELECTRON; MILK PROTEINS; MOLECULAR SEQUENCE DATA; NEURODEGENERATIVE DISEASES; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 84355161488     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1418     Document Type: Article

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