Protein conformational changes in the bacteriorhodopsin photocycle.

doi:10.1006/jmbi.1999.2589

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

Protein conformational changes in the bacteriorhodopsin photocycle.

Journal of molecular biology - 19 Mar 1999

Subramaniam S, Lindahl M, Bullough P, Faruqi A R, Tittor J, Oesterhelt D, Brown L, Lanyi J, Henderson R

Abstract excerpt

We report a comprehensive electron crystallographic analysis of conformational changes in the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic defects in the photocycle. Specific intermediates that accumulate in the late stages of the photocycle of wild-type bacteriorhodopsin, the single mutants D38R, D96N, D96G, T46V, L93A and F219L, and the triple mutant...

Topics

Bacteriorhodopsins
Crystallography
Electrons
Halobacterium salinarum
Image Processing, Computer-Assisted
Light
Light Signal Transduction
Models, Chemical
Models, Molecular
Mutation
Protein Conformation
Proton Pumps

Source

Open in PubMed

Identifiers

PMID: 10074413
DOI: 10.1006/jmbi.1999.2589

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 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