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

Interhelical hydrogen bonds in the CFTR membrane domain.

Nature structural biology - 1 Jul 2001

Therien A G, Grant F E, Deber C M

Abstract excerpt

Critical mutations in the membrane-spanning domains of proteins cause many human diseases. We report the expression in Escherichia coli of helix-loop-helix segments of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel domain in milligram quantities. Analysis of gel migration patterns of these constructs, in conjunction with circular dichroism spectroscopy, demonstrate that a...

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 Cystic Fibrosis Transmembrane Conductance Regulator
Share to Detergents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Helix-Loop-Helix Motifs

Share to Hydrogen Bonding

Share to Molecular Weight

Share to Static Electricity

Share to Thermodynamics

Source

Identifiers

PMID: 11427889
DOI: 10.1038/89631

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interhelical hydrogen bonds in the CFTR membrane domain.PMID 11427889Read ↗

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

Structural effects of extracellular loop mutations in CFTR helical hairpins.Semantic proximity Read ↗

Structural basis for misfolding at a disease phenotypic position in CFTR: comparison of TM3/4 helix-loop-helix constructs with TM4 peptides.Semantic proximity Read ↗

Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin.Semantic proximity Read ↗

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

Destabilization of the transmembrane domain induces misfolding in a phenotypic mutant of cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

Positional dependence of non-native polar mutations on folding of CFTR helical hairpins.Semantic proximity Read ↗

Multiple Membrane-Cytoplasmic Domain Contacts in the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Mediate Regulation of Channel GatingSemantic proximity Read ↗

Loop sequence dictates the secondary structure of a human membrane protein hairpin.Semantic proximity Read ↗

Interdomain but not intermolecular interactions observed in CFTR channels.Semantic proximity Read ↗

Misfolding of the cystic fibrosis transmembrane conductance regulator and disease.Semantic proximity Read ↗

Alteration of CFTR transmembrane span integration by disease-causing mutations.Semantic proximity Read ↗

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