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Structural features and conformational equilibria of 310-helical peptides in solution by spectroscopic and molecular
B Pispisa1, C Mazzuca, A Palleschi
1Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133, Italy. pispisa@stc.uniroma2.it
Biopolymers
|May 16, 2002
Abstract:
The structural features and conformational equilibria of a series of short, linear Calpha-methylvaline [(alphaMe)Val]-based peptides in methanol were investigated by combining fluorescence resonance energy transfer measurements and molecular mechanics data. IR spectra were employed to determine their secondary structure, which exhibits an intramolecularly H-bonded, 3(10)-helix conformation that is affected by backbone distortions that are enhanced by the shortness of the main chain.