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

Effects of a polar amino acid substitution on helix formation and aggregate size along the detergent-induced peptide folding pathway.

Biochimica et biophysica acta - 1 Feb 2013

Alvares Rohan D A, Tulumello David V, Macdonald Peter M, Deber Charles M, Prosser R Scott

Abstract excerpt

Membrane proteins constitute a significant fraction of the proteome and are important drug targets. While the transmembrane (TM) segments of these proteins are primarily composed of hydrophobic residues, the inclusion of polar residues-either naturally occurring or as a consequence of a disease-related mutation-places a significant folding burden in this environment, potentially impacting bilayer insertion and/or...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Detergents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Diffusion

Share to Lipid Bilayers

Share to Lysine

Share to Magnetic Resonance Spectroscopy

Share to Phosphorylcholine

Share to Sodium Dodecyl Sulfate

Source

Identifiers

PMID: 23031573
DOI: 10.1016/j.bbamem.2012.09.024

Genes

SDS

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

Effects of a polar amino acid substitution on helix formation and aggregate size along the detergent-induced peptide folding pathway.PMID 23031573Read ↗

Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment.Semantic proximity Read ↗

Elucidating Molecular Design Principles for Charge-Alternating Peptides.Semantic proximity Read ↗

Asparagine-mediated self-association of a model transmembrane helix.Semantic proximity Read ↗

Protein-protein interactions in the membrane: sequence, structural, and biological motifs.Semantic proximity Read ↗

Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.Semantic proximity Read ↗

Synergistic interactions between aqueous and membrane domains of a designed protein determine its fold and stability.Semantic proximity Read ↗

Polar mutations in membrane proteins as a biophysical basis for disease.Semantic proximity Read ↗

Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems.Semantic proximity Read ↗

Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants.Semantic proximity Read ↗

Local Bilayer Hydrophobicity Modulates Membrane Protein StabilitySemantic proximity Read ↗

A dual sensor regulates P-glycoprotein’s structural plasticitySemantic proximity Read ↗

Communication: The electrostatic polarization is essential to differentiate the helical propensity in polyalanine mutants.Semantic proximity Read ↗

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