Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Nicola Pavitt"'
Autor:
David Hall, Nicola Pavitt
Publikováno v:
Journal of Crystallographic and Spectroscopic Research. 21:241-245
Calcul par ordinateur des energies de conformation de la molecule, en utilisant plusieurs modeles de representation de cette molecule dans son environnement cristallin. Analyse de l'empilement cristallin, par le calcul des contributions en energie de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e0b5d1b6b0c5d7cc513f3457c040faa
https://doi.org/10.1007/bf01161072
https://doi.org/10.1007/bf01161072
Autor:
David Hall, Nicola Pavitt
Publikováno v:
Journal of Computational Chemistry. 5:441-450
A number of force fields of the molecular mechanics type have been tested for their ability to represent as an energy minimum, the observed crystal structure for three cyclic hexapeptides, cyclo-(-Ala-Ala-Gly-Gly-Ala-Gly-), cyclo-(-Ala-Ala-Gly-Gly-Al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b69d702754725038f50e7ae2c8fd684
https://doi.org/10.1002/jcc.540050504
https://doi.org/10.1002/jcc.540050504
Autor:
Nicola Pavitt, David Hall
Publikováno v:
Biopolymers. 23:1441-1455
A systematic survey has been made, using molecular mechanics, of the conformation of cyclo(-Nγ-Mabu-Gly-Ala-Ala-), where Mabu is (R)-α-methyl-γ-aminobutyric acid. This molecule corresponds to the 14-membered ring of the conformationally restricted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42474a5653560d4b8717dd3a5dc8f01b
https://doi.org/10.1002/bip.360230802
https://doi.org/10.1002/bip.360230802
Publikováno v:
Journal of Computational Chemistry. 3:381-384
The conformation of the depsipeptide pithomycolide has been deduced by systematically generating possible models for the molecule, and minimizing their conformation energy. Only one of low-energy solutions is consistent with the reported NMR data.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e133a6ad9db3048c20fab15a31f6991
https://doi.org/10.1002/jcc.540030313
https://doi.org/10.1002/jcc.540030313
Publikováno v:
Journal of Computational Chemistry. 4:114-122
The MM2 molecular mechanics force field, as modified for halogens, is able to predict the structures, dipole moments, and energies of the isomers of benzene hexachloride. For benzene tetrachloride and naphthalene tetrachloride the field exaggerates t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b78ecb328153adde7e941d3cd88255db
https://doi.org/10.1002/jcc.540040116
https://doi.org/10.1002/jcc.540040116
Publikováno v:
Journal of Computational Chemistry. 3:89-94
The conformation of the cyclic pentapeptide malformin A has been deduced by systematically generating possible models for the molecule, and minimizing the conformation energy of each. Only one of the low-energy solutions is fully consistent with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::28462745224a339d98f538a115d62fb4
https://doi.org/10.1002/jcc.540030114
https://doi.org/10.1002/jcc.540030114
Autor:
David Hall, Nicola Pavitt
Publikováno v:
Biopolymers. 23(11 Pt 1)
A systematic survey has been made, using molecular mechanics, of the conformation of the ring entity of the enkephalin analogs, [D-Cys2-L-Cys5]-enkephalinamide and [D-Cys2-D-Cys5]enkephalinamide. These molecules are considerably more flexible than th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edf8ea57ae514fd845e1893980e86439
https://pubmed.ncbi.nlm.nih.gov/6498304
https://pubmed.ncbi.nlm.nih.gov/6498304
Autor:
Nicola Pavitt, David Hall
Publikováno v:
Biopolymers. 24(6)
A comparative study has been made using molecular mechanics of the ring entity of the active enkephalin analogs, Tyr-cyclo(-Nω-D-XXX-Gly-Phe-Leu-), where XXX is variously A2pr, A2bu, and Orn. Several conformations are favored for all three, and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ea8d649107eb38af4937363b84ff3f
https://pubmed.ncbi.nlm.nih.gov/4027340
https://pubmed.ncbi.nlm.nih.gov/4027340