Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Membrane structure of the human immunodeficiency virus gp41 fusion peptide by molecular dynamics simulation. II. The glycine mutants.

Biochimica et biophysica acta - 10 Jan 2003

Wong Tuck C

Abstract excerpt

In this work, molecular dynamics (MD) simulation of the interaction of three mutants, G3V, G5V and G10V, of the human immunodeficiency virus (HIV) gp41 16-residue fusion peptide (FP) with an explicit palmitoyloleoylphosphatidyl-ethanolamine (POPE) lipid bilayer was performed. The goals of this work are to study the correlation of the fusogenic activity of the FPs with the mode of their interaction with the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Glycine
Share to HIV Envelope Protein gp41
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 12507757
DOI: 10.1016/s0005-2736(02)00652-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Membrane structure of the human immunodeficiency virus gp41 fusion peptide by molecular dynamics simulation. II. The glycine mutants.PMID 12507757Read ↗

Membrane structure of the human immunodeficiency virus gp41 fusion domain by molecular dynamics simulation.Semantic proximity Read ↗

Role of the Specific Amino Acid Sequence of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 in Membrane FusionSemantic proximity Read ↗

Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide.Semantic proximity Read ↗

Biochemistry and Biophysics of HIV-1 gp41 - Membrane Interactions and Implications for HIV-1 Envelope Protein Mediated Viral-Cell Fusion and Fusion Inhibitor DesignSemantic proximity Read ↗

The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function.Semantic proximity Read ↗

Structural and Functional Analysis of Interhelical Interactions in the Human Immunodeficiency Virus Type 1 gp41 Envelope Glycoprotein by Alanine-Scanning MutagenesisSemantic proximity Read ↗

Molecular mechanism of HIV-1 gp120 mutations that reduce CD4 binding affinity.Semantic proximity Read ↗

Mutations of conserved glycine residues within the membrane-spanning domain of human immunodeficiency virus type 1 gp41 can inhibit membrane fusion and incorporation of Env onto virions.Semantic proximity Read ↗

Interhelical Interactions in the gp41 Core: Implications for Activation of HIV-1 Membrane Fusion<sup>,</sup>Semantic proximity Read ↗

The fusion activity of HIV-1 gp41 depends on interhelical interactions.Semantic proximity Read ↗

The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: a novel fusogenic sequence.Semantic proximity Read ↗

The conserved glycine residues in the transmembrane domain of the Semliki Forest virus fusion protein are not required for assembly and fusion.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.