Folding Molecular Dynamics Simulation of a gp41-Derived Peptide Reconcile Divergent Structure Determinations
Author:
Affiliation:
1. Department of Molecular Biology and Genetics, Democritus University of Thrace, University Campus, Alexandroupolis 68100, Greece
Publisher
American Chemical Society (ACS)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acsomega.8b01579
Reference65 articles.
1. A Conserved Tryptophan-Rich Motif in the Membrane-Proximal Region of the Human Immunodeficiency Virus Type 1 gp41 Ectodomain Is Important for Env-Mediated Fusion and Virus Infectivity
2. Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure
3. A Synthetic Peptide from HIV-1 gp41 Is a Potent Inhibitor of Virus-Mediated Cell—Cell Fusion
4. HIV-1 Membrane Fusion Mechanism: Structural Studies of the Interactions between Biologically-Active Peptides from gp41
5. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
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1. Folding molecular dynamics simulation of T‐peptide, a HIV viral entry inhibitor: Structure, dynamics, and comparison with the experimental data;Journal of Computational Chemistry;2022-03-25
2. A molecular dynamics simulation study on the propensity of Asn-Gly-containing heptapeptides towards β-turn structures: Comparison with ab initio quantum mechanical calculations;PLOS ONE;2020-12-03
3. Molecular simulation of peptides coming of age: Accurate prediction of folding, dynamics and structures;Archives of Biochemistry and Biophysics;2019-03
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