Structural features and conformational equilibria of 310-helical peptides in solution by spectroscopic and molecular mechanics studies.
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.
Pispisa
B
B
Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133, Italy. pispisa@stc.uniroma2.it
Mazzuca
C
C
Palleschi
A
A
Stella
L
L
Venanzi
M
M
Formaggio
F
F
Toniolo
C
C
Broxterman
Q B
QB
D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012984:Software; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry / Q000379:methods*; D013997:Time Factors
D010455:Peptides