FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin.

doi:10.1021/bi050122+

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

FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin.

Biochemistry - 24 May 2005

Shibata Mikihiro, Kandori Hideki

Abstract excerpt

In a light-driven proton pump protein, bacteriorhodopsin (BR), three water molecules participate in a pentagonal cluster that stabilizes an electric quadrupole buried inside the protein. Previously, low-temperature Fourier-transform infrared (FTIR) difference spectra between BR and the K photointermediate in D(2)O revealed six O-D stretches of water in BR at 2690, 2636, 2599, 2323, 2292, and 2171 cm(-)(1), while...

Topics

Archaeal Proteins
Arginine
Aspartic Acid
Bacteriorhodopsins
Cytoplasm
Halobacterium salinarum
Hydrogen Bonding
Mutation
Proton Pumps
Schiff Bases
Spectroscopy, Fourier Transform Infrared
Thermodynamics
Water

Source

Open in PubMed

Identifiers

PMID: 15895984
DOI: 10.1021/bi050122+

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