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

Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin.

Biochemistry - 19 Jun 2007

Wehbi Hania, Rath Arianna, Glibowicka Mira, Deber Charles M

Abstract excerpt

The folding of membrane-spanning domains into their native functional forms depends on interactions between transmembrane (TM) helices joined by covalent loops. However, the importance of these covalent linker regions in mediating the strength of helix-helix associations has not been systematically addressed. Here we examine the potential structural impact of cystic fibrosis-phenotypic mutations in the...

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

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

Share to Electrophoresis, Polyacrylamide Gel

Share to In Vitro Techniques

Share to Peptide Fragments

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Static Electricity

Source

Identifiers

PMID: 17516627
DOI: 10.1021/bi602570u

Genes

CFTR
SDS

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin.PMID 17516627Read ↗

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

Interhelical hydrogen bonds in the CFTR membrane domain.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 ↗

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

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

Dynamics of the Second Extracellular Loop Control Transducer Coupling of Peptide-Activated GPCRs.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 ↗

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

Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion.Semantic proximity Read ↗

Formation of helical hairpins during membrane protein integration into the endoplasmic reticulum membrane. Role of the N and C-terminal flanking regions.Semantic proximity Read ↗

The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bonds.Semantic proximity Read ↗

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