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Titolo:
500PICOSECOND MOLECULAR-DYNAMICS SIMULATION OF AMPHIPHILIC POLYPEPTIDE AC(LKKL)(4) NHET WITH 1,2-DI-MYSRISTOYL-SN-GLYCERO-3-PHOSPHORYLCHOLINE (DMPC) MOLECULES
Autore:
GUPTA D; KOTHEKAR V;
Indirizzi:
ALL INDIA INST MED SCI,DEPT BIOPHYS,MOL MODELING LAB NEW DELHI 110029INDIA
Titolo Testata:
Indian Journal of Biochemistry & Biophysics
fascicolo: 6, volume: 34, anno: 1997,
pagine: 501 - 511
SICI:
0301-1208(1997)34:6<501:5MSOAP>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CORTICOTROPIN-RELEASING-FACTOR; SMALL UNILAMELLAR VESICLES; PHOSPHOLIPID-BILAYER; STRUCTURAL FLUCTUATIONS; HELICOIDAL PARAMETERS; LIPID-MEMBRANES; PEPTIDES; PROTEINS; ORIENTATION; SURFACE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
D. Gupta e V. Kothekar, "500PICOSECOND MOLECULAR-DYNAMICS SIMULATION OF AMPHIPHILIC POLYPEPTIDE AC(LKKL)(4) NHET WITH 1,2-DI-MYSRISTOYL-SN-GLYCERO-3-PHOSPHORYLCHOLINE (DMPC) MOLECULES", Indian Journal of Biochemistry & Biophysics, 34(6), 1997, pp. 501-511

Abstract

Molecular dynamics (MD) simulation of the interaction between amphiphilic polypeptide Ac(LKKL)(4)NHEt and 4 DMPC (1, 2 di-mysristoyl-sn-glycero-3-phosphorylcholine) molecules has been carried out at 310 K for 500 picoseconds (ps) using AMBER 4.0. Interaction energy and a number of conformational parameters are calculated for the subaveraged coordinates, using P-CURVES 3.1 and our MD trajectory analysis program ANALMD. No significant change in DMPC headgroup conformation was observed. However, the mobility of P atoms was found to be restricted. The chains were quite flexible and their flexibility increased towards the ends. They interacted amongst themselves. The polypeptide remained predominantly in a-helical conformation. Leu1 and Lys2 at the N terminus and Leu13 to Leu16 at C terminus assumed non helical conformation and werequite flexible. Average interaction energy between the polypeptide and DMPC molecules was found to be -151.828 kcal()mol(-1). The main contributory factor was electrostatic interaction of Lys NH3+ groups withthe DMPC phosphates. On an average one Lys chain interacted with 1.5 DMPC molecules. Central region of the polypeptide had better contact with DMPC molecules. A model for the fusogenic properties of the polypeptide is presented on the basis of MD results.

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Documento generato il 30/09/20 alle ore 05:35:19