ArticleBiochemistry2009
Active water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Atomic insights into the signaling landscape of E. coli PhoQ histidine kinase from molecular dynamics simulations.Scientific reports · 2024Article
- Article
- Visualizing water molecules in transmembrane proteins using radiolytic labeling methods.Biochemistry · 2010Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We detect internal water molecules in a membrane-embedded receptor-transducer complex and demonstrate water structure changes during formation of the signaling state. Time-resolved FTIR spectroscopy reveals stimulus-induced repositioning of one or more structurally active water molecules to a significantly more hydrophobic environment in the signaling state of the sensory rhodopsin II (SRII)-transducer (HtrII) complex. These waters, distinct from bound water molecules within the SRII receptor, appear to be in the middle of the transmembrane interface region near the Tyr199(SRII)-Asn74(HtrII) hydrogen bond. We conclude that water potentially plays an important role in the SRII --> HtrII signal transfer mechanism in the membrane's hydrophobic core.
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Registered trials
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