title: Structural features and conformational equilibria of 310-helical peptides in solution by spectroscopic and molecular mechanics studies.
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.
authors.affiliation: Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133, Italy. pispisa@stc.uniroma2.it
authors.forename: B
authors.initials: B
authors.lastname: Pispisa
authors.forename: C
authors.initials: C
authors.lastname: Mazzuca
authors.forename: A
authors.initials: A
authors.lastname: Palleschi
authors.forename: L
authors.initials: L
authors.lastname: Stella
authors.forename: M
authors.initials: M
authors.lastname: Venanzi
authors.forename: F
authors.initials: F
authors.lastname: Formaggio
authors.forename: C
authors.initials: C
authors.lastname: Toniolo
authors.forename: Q B
authors.initials: QB
authors.lastname: Broxterman
mesh_terms: 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
chemical_list: D010455:Peptides