Random coils, β-sheet ribbons, and α-helical fibers: One peptide adopting three different secondary structures at will

Journal of the American Chemical Society

Volumn 128, Issue 7, 2006, Pages 2196-2197

  Pagel, Kevin ^a   Wagner, Sara C ^a   Samedov, Kerim ^a   Von Berlepsch, Hans ^a   Böttcher, Christoph ^a   Koksch, Beate ^a  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE;

ALPHA HELIX; ALZHEIMER DISEASE; ARTICLE; BETA SHEET; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DEGENERATIVE DISEASE; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; OXIDATIVE STRESS; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 33644533148     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja057450h     Document Type: Article

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