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Titolo:
260 PS MOLECULAR-DYNAMICS SIMULATION OF SUBSTANCE-P WITH HYDRATED DIMYRISTOYL PHOSPHATIDYL CHOLINE BILAYER
Autore:
KOTHEKAR V;
Indirizzi:
ALL INDIA INST MED SCI,DEPT BIOPHYS NEW DELHI 110029 INDIA
Titolo Testata:
Journal of biomolecular structure & dynamics
fascicolo: 4, volume: 13, anno: 1996,
pagine: 601 - 613
SICI:
0739-1102(1996)13:4<601:2PMSOS>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIPID BILAYER; CONFORMATIONAL-ANALYSIS; SECONDARY STRUCTURE; ENERGY CALCULATIONS; PEPTIDE-HORMONES; AQUEOUS-SOLUTION; CYCLIC ANALOGS; MEMBRANES; WATER; NMR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
60
Recensione:
Indirizzi per estratti:
Citazione:
V. Kothekar, "260 PS MOLECULAR-DYNAMICS SIMULATION OF SUBSTANCE-P WITH HYDRATED DIMYRISTOYL PHOSPHATIDYL CHOLINE BILAYER", Journal of biomolecular structure & dynamics, 13(4), 1996, pp. 601-613

Abstract

We present here results on 260 pico seconds (ps) molecular dynamics (MD) simulation of substance P (SP) in hydrated bilayer of dimyristoyl phosphatidyl choline (DMPC) (39 molecules of DMPC with 776 water molecules). 260 ps MD simulation has been carried out in 0.001 ps time interval with united atom force field, using AMBER 4.0 package. Non bondedpair list was updated every 20 cycles using 12.5 Angstrom cut off distance. Analysis of MD data is done using our package ANALMD. The obtained models are Presented using graphics package RASMOL. All simulations, analysis of MD data and graphics is done on INDIGO-2, R-4400 extreme graphics work station. Our results show no systematic change in order parameter, but reduction in transfraction of the chain torsional angles, compared to our earlier results on MD simulation on hydrated DMPCbilayer without SP. C-terminal and central peptide residues adopt partial helical conformation. Helix type as classified on the basis of H-bonds is between alpha and 3(10). The peptide backbone shows flexibility during heating runs. Later, it is stabilized and there was not muchchange in the spatial position of the backbone. Lipid matrix serves the role of immobilization of the peptide backbone in a preferred conformation.

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Documento generato il 30/09/20 alle ore 05:57:58