Use of a designed triple-stranded antiparallel β-sheet to probe β-sheet cooperativity in aqueous solution

Journal of the American Chemical Society

Volumn 120, Issue 19, 1998, Pages 4869-4870

  Schenck, Heather L ^a   Gellman, Samuel H ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0043122630     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja973984+     Document Type: Article

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30. After our studies were completed, a related paper appeared: Sharman, G. J.; Searle, M. S. J. Chem. Soc., Chem. Commun. 1997, 1955. These workers describe a 24-residue sequence, containing two NG turn segments, that adopts a triple-stranded antiparallel ǎ-sheet in 50% aqueous methanol. This peptide does not appear to display ǎ-sheet folding in the absence of an organic solvent.