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

A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer.

Biochimica et biophysica acta - 1 Sept 2012

Weber Mathias, Tome Lydia, Otzen Daniel, Schneider Dirk

Abstract excerpt

When localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b(559)' to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane...

Read the complete abstract on PubMed

Topics

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

Share to Cytochrome b Group
Share to Heme
Share to Hydrogen Bonding

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

Share to Molecular Conformation

Share to Oxygen

Share to Photosystem II Protein Complex

Share to Proline

Share to Spectrophotometry

Source

Identifiers

PMID: 22525600
DOI: 10.1016/j.bbamem.2012.04.003

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

A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer.PMID 22525600Read ↗

Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochrome bc1 perturbs heme bH redox potential and spin state.Semantic proximity Read ↗

The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.Semantic proximity Read ↗

A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin.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 ↗

A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket.Semantic proximity Read ↗

A mutational study of transmembrane helix-helix interactions.Semantic proximity Read ↗

Hydrogen bond network of cytochrome P-450cam: a network connecting the heme group with helix K.Semantic proximity Read ↗

Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.Semantic proximity Read ↗

Role of His residues in Bacillus subtilis cytochrome b558 for haem binding and assembly of succinate: quinone oxidoreductase (complex II).Semantic proximity Read ↗

Structural impact of proline mutations in the loop region of an ancestral membrane protein.Semantic proximity Read ↗

Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.Semantic proximity Read ↗

X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35-->Tyr mutant.Semantic proximity Read ↗

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