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

Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin.

Biochemistry - 16 Nov 1993

Resek J F, Farahbakhsh Z T, Hubbell W L, Khorana H G

Abstract excerpt

Five mutations of rhodopsin have been produced, each of which contains a unique cysteine residue at positions 62, 65, 140, 240, or 316 in the cytoplasmic domain. The single reactive cysteines were derivatized with a sulfhydryl-specific nitroxide spin-label, and the electron paramagnetic resonance (EPR) spectra were analyzed in both lauryl maltoside and digitonin in the dark and after photobleaching. The collision...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Blotting, Western
Share to Cattle

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

Share to Cysteine

Share to Cytoplasm

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 8218279
DOI: 10.1021/bi00096a012

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

Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin.PMID 8218279Read ↗

Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements.Semantic proximity Read ↗

Rhodopsin deactivation is affected by mutations of Tyrl91.Semantic proximity Read ↗

Protein conformational changes in the bacteriorhodopsin photocycle.Semantic proximity Read ↗

Effect of Outer-Sphere Side Chain Substitutions on the Fate of the trans Iron-Nitrosyl Dimer in Heme/Nonheme Engineered Myoglobins (Fe(B)Mbs): Insights into the Mechanism of Denitrifying NO Reductases.Semantic proximity Read ↗

Highly conserved tyrosine stabilizes the active state of rhodopsin.Semantic proximity Read ↗

Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories.Semantic proximity Read ↗

Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin.Semantic proximity Read ↗

Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the reprotonation mechanism.Semantic proximity Read ↗

The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.Semantic proximity Read ↗

Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin.Semantic proximity Read ↗

Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle.Semantic proximity Read ↗

Different dark conformations function in color-sensitive photosignaling by the sensory rhodopsin I-HtrI complex.Semantic proximity Read ↗

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