Molecular Dynamics Simulation of Cholera Toxin A-1 Polypeptide

Abstract: A molecular dynamics (MD) simulation study of the enzymatic portion of cholera toxin; cholera toxin A-1 polypeptide (CTA1) was performed at 283, 310 and 323 K. From total energy analysis it was observed that this toxin is stable thermodynamically and these outcomes were likewise confirmed by root mean square deviations (RMSD) investigations. The Cα root mean square fluctuation (RMSF) examinations revealed that there are a number of residues inside CTA1, which can be used as target for designing and synthesizing inhibitory drugs, in order to inactivate cholera toxin inside the human body. The fluctuations in the radius of gyration and hydrogen bonding in CTA1 proved that protein unfolding and refolding were normal routine phenomena in its structure at all temperatures. Solvent accessible surface area study identified the hydrophilic nature of the CTA1, and due to this property it can be a potential biological weapon. The structural identification (STRIDE) algorithm for proteins was successfully used to determine the partially disordered secondary structure of CTA1. On account of this partially disordered secondary structure, it can easily deceive the proteolytic enzymes of the endoplasmic reticulum of host cells.

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Englisch

Verweise und Beziehungen

• Erschienen in: Molecular Dynamics Simulation of Cholera Toxin A-1 Polypeptide ; volume:14 ; number:1 ; year:2016 ; pages:188-196 ; extent:9 ; Open chemistry ; 14, Heft 1 (2016), 188-196 (gesamt 9)

Beteiligte, Orts- und Zeitangaben

• Urheber: Badshah, Syed Lal ; Khan, Abdul Naeem ; Mabkhot, Yahia Nasser

Weitere Informationen

• DOI: 10.1515/chem-2016-0021
• URN: urn:nbn:de:101:1-2410161548585.730869363726
• Rechteinformation: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 15.08.2025, 07:28 MESZ