Distinguishing helix conformations in alanine-rich peptides using the unnatural amino acid TOAC and electron spin resonance

Journal of the American Chemical Society

Volumn 118, Issue 1, 1996, Pages 271-272

  Hanson, Paul ^a   Martinez, Gary ^a   Millhauser, Glenn ^a   Formaggio, Fernando ^b   Crisma, Marco ^b   Toniolo, Claudio ^b   Vita, Claudio ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF PADOVA   (Italy)

^c CE Saclay ^*  (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE DERIVATIVE; HEXAPEPTIDE;

ARTICLE; ELECTRON SPIN RESONANCE; PROTEIN STRUCTURE; SPIN LABELING;

EID: 0030066039     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja952423k     Document Type: Article

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27. Smythe et al. (J. Am. Chem. Soc. 1995, 117, 10555-10562) have recently reported similar studies on TOAC-labeled peptides. Despite reaching similar conclusions, we offer a fundamentally different interpretation of the role TOAC plays in stabilizing helix structure.