Abstract
The fully Cα-methylated homo-peptide Ac-[l-(αMe)Val]7-NHiPr is completely 310-helical when its crystals are grown from a methanol solution, whereas it is α-helical when crystallized from HFIP (1,1,1,3,3,3-hexafluoropropan-2-ol), thus providing an example of a solvent-driven α/310-helix dimorphism in the crystal state. The interactions of cocrystallized HFIP molecules with the peptide in the α-helical structure are reported.
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