ArticleProtein science : a publication of the Protein Society2008
Buried water molecules in helical transmembrane proteins.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Functional role of a structural water in the elevator domain of dicarboxylate transporter VcINDY.PNAS nexus · 2026Article
- Water molecules mediate zinc mobility in the bacterial zinc diffusion channel ZIPB.The Journal of biological chemistry · 2019Article
- Using X-ray Footprinting and Mass Spectrometry to Study the Structure and Function of Membrane Proteins.Protein and peptide letters · 2019Review
- Synchrotron X-ray footprinting as a method to visualize water in proteins.Journal of synchrotron radiation · 2016Article
- The G protein-coupled receptor rhodopsin: a historical perspective.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Copper-transporting P-type ATPases use a unique ion-release pathway.Nature structural & molecular biology · 2014Article
- A hybrid structural approach to analyze ligand binding by the serotonin type 4 receptor (5-HT4).Molecular & cellular proteomics : MCP · 2013Article
- A peptide's perspective of water dynamics.Chemical physics · 2011Article
- Transmembrane helical domain of the cannabinoid CB1 receptor.Biophysical journal · 2009Article
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1 author at 1 institution in 1 country.
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Abstract
Buried water molecules (having no contact with bulk solvent) in 30 helical transmembrane (TM) protein structures were identified. The average amount of buried water in helical TM proteins is about the same as for all water-soluble (WS) proteins, but it is greater than the average for helical WS proteins. Buried waters in TM proteins make more polar contacts, and are more frequently found contacting helices than in WS proteins. The distribution of the buried water binding sites across the membrane profile shows that the sites to some extent reflect protein function. There is also evidence for asymmetry of the sites, with more in the extracellular half of the membrane. Many of the buried water contact sites are conserved across families of proteins, including family members having different functions. This suggests that at least some buried waters play a role in structural stabilization. Disease-causing mutations, which are known to result in misfolded TM proteins, occur at buried water contact sites at a higher than random frequency, which also supports a stabilizing role for buried water molecules.
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