The roles of turn formation and cross-strand interactions in fibrillization of peptides derived from the OspA single-layer β-sheet

Protein Science

Volumn 10, Issue 10, 2001, Pages 2083-2092

  Ohnishi, Satoshi ^a   Koide, Akiko ^a   Koide, Shohei ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

hairpin; Sheet; Fibril formation; Folding; Peptide design

Indexed keywords

AMYLOID; BACTERIAL PROTEIN; OUTER SURFACE PROTEIN A; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; BORRELIA; CONFORMATIONAL TRANSITION; FIBER; HOLLIDAY JUNCTION; HYDROPHILICITY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; TEMPERATURE DEPENDENCE;

ANTIGENS, SURFACE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; BACTERIAL VACCINES; BORRELIA; KINETICS; LIPOPROTEINS; LYME DISEASE VACCINES; MODELS, MOLECULAR; PEPTIDES; PRECIPITATION; PROTEIN STRUCTURE, SECONDARY;

EID: 0034808069     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.15901     Document Type: Article

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