A peptide study of the relationship between the collagen triple-helix and amyloid

Biopolymers

Volumn 97, Issue 10, 2012, Pages 795-806

  Parmar, Avanish S ^a,b   Nunes, Ana Monica ^c   Baum, Jean ^c   Brodsky, Barbara ^a,b  

^a Tufts University   (United States)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

aggregation; amyloid; CD; collagen; light scattering; NMR; triple helix

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID; AMYLOID FIBRIL; AMYLOID FIBRIL ELONGATION; AMYLOID FIBRIL FORMATION; AMYLOID FIBRIL GROWTH; AMYLOID PLAQUES; AMYLOIDOGENESIS; AMYLOIDOGENIC PEPTIDES; CD; COLLAGEN TRIPLE HELIX; CONFORMATIONAL CHANGE; HELICAL PEPTIDE; HYBRID PEPTIDES; INHIBITORY EFFECT; NMR DATA; PEPTIDE MODELS; RANDOM-COIL STRUCTURES; TRIPLE HELIX CONFORMATION; TRIPLE HELIXES;

AGGLOMERATION; COLLAGEN; CONFORMATIONS; GLYCOPROTEINS; LIGHT SCATTERING; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEATION;

PEPTIDES;

AMYLOID; COLLAGEN; COLLAGEN TYPE XXV; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; INHIBITION KINETICS; LIGHT SCATTERING; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PROTEIN AGGREGATION; PROTEIN DOMAIN; REGULATORY MECHANISM; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; TRIPLE HELIX;

AMINO ACID SEQUENCE; AMYLOID; CIRCULAR DICHROISM; COLLAGEN; MICROSCOPY, ELECTRON; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; SCATTERING, RADIATION;

EID: 84863937895     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.22070     Document Type: Article

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