The fully C-alpha-methylated homo-peptide Ac-[L-(alpha Me)Val](7)-NHiPr is completely 3(10)-helical when its crystals are grown from a methanol solution, whereas it is alpha-helical when crystallized from HFIP (1,1,1,3,3,3-hexafluoropropan-2-ol), thus providing an example of a solvent-driven alpha/3(10)-helix dimorphism in the crystal state. The interactions of cocrystallized HFIP molecules with the peptide in the alpha-helical structure are reported.

Peptide alpha/3(10)-helix dimorphism in the crystal state

Marco Crisma;Michele Saviano;Alessandro Moretto;Claudio Toniolo
2007

Abstract

The fully C-alpha-methylated homo-peptide Ac-[L-(alpha Me)Val](7)-NHiPr is completely 3(10)-helical when its crystals are grown from a methanol solution, whereas it is alpha-helical when crystallized from HFIP (1,1,1,3,3,3-hexafluoropropan-2-ol), thus providing an example of a solvent-driven alpha/3(10)-helix dimorphism in the crystal state. The interactions of cocrystallized HFIP molecules with the peptide in the alpha-helical structure are reported.
2007
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/144121
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