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

The most highly amphiphilic α‐helices include two amino acid segments in human immunodeficiency virus glycoprotein 41

1 Jan 1990

Abstract excerpt

A search for highly amphiphilic alpha-helices has been made in a data base of protein sequences, using the helical hydrophobic moment as a criterion of amphiphilicity. The protein segments of largest hydrophobic moment have been analyzed. For the segments whose structures are known, they are in fact alpha-helices. Two of the segments having very large hydrophobic moments are from the smaller C-terminal portion of...

Read the complete abstract on PubMed

Topics

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

Share to Antimicrobial Peptides and Activities
Share to Biochemical and Structural Characterization
Share to Healthcare and Venom Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 2328285
DOI: 10.1002/bip.360290122

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

The most highly amphiphilic α‐helices include two amino acid segments in human immunodeficiency virus glycoprotein 41PMID 2328285Read ↗

Amphiphilic α-helical potential: a putative folding motif adding few constraints to protein evolution.Semantic proximity Read ↗

Hydrophobic substitutions in the first residue of the CRAC segment of the gp41 protein of HIV.Semantic proximity Read ↗

An Immunodominant Epitope of Myelin Basic Protein Is an Amphipathic α-HelixSemantic proximity Read ↗

Membrane interactions of synthetic peptides corresponding to amphipathic helical segments of the human immunodeficiency virus type-1 envelope glycoprotein.Semantic proximity Read ↗

Two conserved residues are important for inducing highly ordered membrane domains by the transmembrane domain of influenza hemagglutinin.Semantic proximity Read ↗

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

Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat antibiotic resistance in bacterial infection.Semantic proximity Read ↗

Functional and Structural Characterization of HIV-1 gp41 Ectodomain Regions in Phospholipid Membranes Suggests that the Fusion-active Conformation Is ExtendedSemantic proximity Read ↗

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