The structural features and conformational equilibria of a series of short, linear Cα-methylvaline [(αMe)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, 310-helix conformation that is affected by backbone distortions that are enhanced by the shortness of the main chain
Pispisa, B., Mazzuca, C., Palleschi, A., Stella, L., Venanzi, M., Formaggio, F., et al. (2002). Structural features and conformational equilibria of 3,10-helical peptides in solution by spectroscopic and molecular mechanics studies. BIOPOLYMERS, 67, 247-250 [10.1002/bip.10118].
Structural features and conformational equilibria of 3,10-helical peptides in solution by spectroscopic and molecular mechanics studies
PISPISA, BASILIO;MAZZUCA, CLAUDIA;PALLESCHI, ANTONIO;STELLA, LORENZO;VENANZI, MARIANO;
2002-01-01
Abstract
The structural features and conformational equilibria of a series of short, linear Cα-methylvaline [(αMe)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, 310-helix conformation that is affected by backbone distortions that are enhanced by the shortness of the main chainI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.