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Titolo:
SUBSTITUTION BY GLU FOR RESTRICTING THE CONFORMATIONAL FREEDOM OF LYS-XAA FRAGMENTS IN BIOACTIVE PEPTIDES BY SIDE-CHAIN LACTAMIZATION
Autore:
KOSTETSKY PV; ARTEMEV IV;
Indirizzi:
RUSSIAN ACAD SCI,SHEMYAKIN & OVCHINNIKOV INST BIOORGAN CHEM MOSCOW 117871 RUSSIA
Titolo Testata:
Molecular biology
fascicolo: 3, volume: 32, anno: 1998,
pagine: 410 - 416
SICI:
0026-8933(1998)32:3<410:SBGFRT>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORMONE RELEASING-FACTOR; CYCLIC LACTAM ANALOGS; MOLECULAR-DYNAMICS; CENTRAL RECEPTORS; SIMULATIONS; DESIGN; NMR; TETRAPEPTIDES; THYMOPOIETIN; SPECTROSCOPY;
Keywords:
CYCLIC DIPEPTIDE; THEORETICAL CONFORMATIONAL ANALYSIS; THYMOPENTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
P.V. Kostetsky e I.V. Artemev, "SUBSTITUTION BY GLU FOR RESTRICTING THE CONFORMATIONAL FREEDOM OF LYS-XAA FRAGMENTS IN BIOACTIVE PEPTIDES BY SIDE-CHAIN LACTAMIZATION", Molecular biology, 32(3), 1998, pp. 410-416

Abstract

Using the cyclic peptide Ac-Lys-Glu-NHMe as an example, the possibility of using lactamization of the neighboring Lys and Glu residues to restrict the conformational mobility has been examined. As shown by thecalculation methods, the lactam can assume quite many conformations, of which 33 correspond to nine low-energy regions of the linear dipeptide Ac-Ala-Ala-NHMe. In the latter case, the structural variability ofthe Lys residue is limited to two regions (A+G and C+F in the Zimmerman-Scheraga nomenclature) on the phi,psi map. The dihedral angles phi and psi of the Glu residue may be found in the majority of the conformational map regions corresponding to the low-energy regions of an Ala residue.

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Documento generato il 12/07/20 alle ore 06:52:09