A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.

doi:10.1021/jacs.6b03681

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

Back to search

Article

A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.

Journal of the American Chemical Society - 20 Jul 2016

Nosrati Meisam, Berbasova Tetyana, Vasileiou Chrysoula, Borhan Babak, Geiger James H

Abstract excerpt

The members of the rhodopsin family of proteins are involved in many essential light-dependent processes in biology. Specific photoisomerization of the protein-bound retinylidene PSB at a specified wavelength range of light is at the heart of all of these systems. Nonetheless, it has been difficult to reproduce in an engineered system. We have developed rhodopsin mimics, using intracellular lipid binding protein...

Topics

Biomimetic Materials
Humans
Isomerism
Models, Molecular
Molecular Conformation
Mutation
Photochemical Processes
Protein Conformation
Protein Engineering
Receptors, Retinoic Acid
Rhodopsin

Source

Open in PubMed Open full text

Identifiers

PMID: 27310917
DOI: 10.1021/jacs.6b03681
PMCID: PMC7780486

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics