Synthesis, and crystal and molecular structure of the 310-helical ?,?-dehydro pentapeptide Boc-Leu-Phe-Ala-?Phe-Leu-Ome

1 intramolecular hydrogen bonds, characteristic of 3(10)-helix. In the crystal, the peptide helices interact through two head-to-tail, N-H-O intermolecular hydrogen bonds. The peptide molecules related by 2(1) screw symmetry form a skewed assembly of helices. -->
ISSN: 1097-0282
0006-3525
DOI: 10.1002/bip.360350202
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_________::e1d960664648efc644f4143b0270405e
https://doi.org/10.1002/bip.360350202
Rights: CLOSED
Přírůstkové číslo: edsair.doi...........e1d960664648efc644f4143b0270405e
Autor: R. M. Jain, Virander S. Chauhan, Tapas K. Mal, K. R. Rajashankar, Suryanarayanarao Ramakumar
Rok vydání: 1995
Předmět:
Zdroj: Biopolymers. 35:141-147
ISSN: 1097-0282
0006-3525
DOI: 10.1002/bip.360350202
Popis: alpha,beta-Dehydro amino acid residues are known to constrain the peptide backbone to the beta-bend conformation. A pentapeptide containing only one alpha,beta-dehydrophenylalanine (delta Phe) residue has been synthesized and crystallized, and its solid state conformation has been determined. The pentapeptide Boc-Leu-Phe-Ala-delta Phe-Leu-OMe (C39H55N5O8, Mw = 721.9) was crystallized from aqueous methanol. Monoclinic space group was P2(1), a = 10.290(2) degrees, b = 17.149(2) degrees, c = 12.179(2) A, beta = 96.64(1) degrees with two molecules in the unit cell. The x-ray (MoK alpha, lambda = 0.7107A) intensity data were collected using a CAD4 diffractometer. The crystal structure was determined by direct methods and refined using least-squares technique. R = 4.4% and Rw = 5.4% for 4403 reflections having magnitude of F0 > or = 3 sigma(magnitude of F0). All the peptide links are trans and the pentapeptide molecule assumes 3(10)-helical conformation. The mean phi,psi values, averaged over the first four residues, are -64.4 degrees, -22.4 degrees respectively. There are three 4-->1 intramolecular hydrogen bonds, characteristic of 3(10)-helix. In the crystal, the peptide helices interact through two head-to-tail, N-H-O intermolecular hydrogen bonds. The peptide molecules related by 2(1) screw symmetry form a skewed assembly of helices.
Databáze: OpenAIRE
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