Repozytorium
Wyszukaj
Kolekcje
Inne
Comparison of fully optimized α-and 310-helices with extended β-strands. An ONIOM density functional theory study.
Autorzy
Rok wydania
2004
Czasopismo
Journal of the American Chemical Society
Numer woluminu
126
Strony
14198-14205
DOI
10.1021/ja048831i
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
We compare the structures and energies of β-strands, α-helices, and 310-helices for capped polyalanines, acetyl(ala)NNH2, for values of N from 2 to 18, using completely optimized mixed DFT/AM1 calculations. Non-pairwise additive cooperativity is manifest from the variation of the relative energies, helical strain, dipole moments, and H-bond lengths of both types of helices, but especially for the α-helices. While the gas-phase 310-helices are more stable for small polyalanines, largely due to the additional H-bond, the α-helices become relatively more stable as the polyalanines increase in size.
Słowa kluczowe
Chemical structure, Cooperativity, Energy, Molecular structure, Peptides and proteins
Adres publiczny
https://doi.org/10.1021/ja048831i
Strona internetowa wydawcy
Podobne publikacje
Enthalpies of hydrogen-bonds in α-helical peptides. An ONIOM DFT/AM1 study.
Wieczorek Robert, Dannenberg J. J.
H-bonding cooperativity and energetics of α-helix formation of five 17-amino acid peptides.
Wieczorek Robert, Dannenberg J. J.