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Volumn 12, Issue 5, 2011, Pages 1781-1794

Heterogeneous triangular structures of human islet amyloid polypeptide (Amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

3-FOLD SYMMETRY; AMYLOID FIBRIL; ATOMIC LEVELS; BIOPHYSICAL DATA; CONFORMATION SEARCH; CROSS SECTION; EXPERIMENTAL DATA; EXPLICIT SOLVENTS; FIBRIL GROWTH; HUMAN ISLETS; HYDROPHOBIC CAVITIES; HYDROPHOBIC CORE; LAYER ASSEMBLY; MISFOLDING; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR ORIGINS; PEPTIDE ELONGATION; POLYMORPHIC STRUCTURE; SANDWICH MODEL; SOLID STATE NMR; STRUCTURAL FEATURE; STRUCTURAL STABILITIES; TRIANGULAR STRUCTURES; TWO-DIMENSION; TYPE II;

EID: 79955852760     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm2001507     Document Type: Article
Times cited : (33)

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