Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed 13C solid-state NMR spectroscopy

Magnetic Resonance in Chemistry

Volumn 42, Issue 2, 2004, Pages 247-257

  Naito, Akira ^a   Kamihira, Miya ^b   Inoue, Ryozo ^b   Saitô, Hazime ^b  

^a YOKOHAMA NATIONAL UNIVERSITY   (Japan)

^b UNIVERSITY OF HYOGO   (Japan)

Author keywords

13C NMR; Amyloid fibril; Autocatalytic reaction; Chemical shifts; Human calcitonin; Interatomic distance; NMR; REDOR

Indexed keywords

CHAINS; GLYCOPROTEINS; LIGHT POLARIZATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; RATE CONSTANTS;

13C NMR; AMYLOID FIBRIL; AUTOCATALYTIC REACTIONS; CHAIN PACKING; FIBRIL FORMATION; HUMAN CALCITONIN; INTER-ATOMIC DISTANCES; RANDOM COIL; REDOR; SOLID-STATE NMR SPECTROSCOPY;

CHEMICAL SHIFT;

AMIDE; AMYLOID; ASPARTIC ACID; CALCITONIN; CARBON 13; HISTIDINE; LYSINE; NITROGEN 15; NITROGEN DERIVATIVE; PENTAPEPTIDE;

ACIDITY; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFERENCE PAPER; CORRELATION ANALYSIS; ISOTOPE LABELING; MOLECULAR MODEL; PH; PROTEIN ANALYSIS; PROTEIN STRUCTURE; SEPARATION TECHNIQUE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

EID: 0842307662     PISSN: 07491581     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrc.1323     Document Type: Conference Paper

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