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- W2922580353 abstract "Transmembrane peptides contain polar residues in the interior of the membrane, which may alter the electrostatic environment and favor hydration in the otherwise nonpolar environment of the membrane core. Here, we demonstrate a general, nonperturbative strategy to probe hydration of the peptide backbone at specific depths within the bilayer using a combination of site-specific isotope labels, ultrafast two-dimensional infrared spectroscopy, and spectral modeling based on molecular dynamics simulations. Our results show that the amphiphilic pH-low insertion peptide supports a highly heterogeneous environment, with significant backbone hydration of nonpolar residues neighboring charged residues. For example, a leucine residue located as far as 1 nm into the hydrophobic bulk reports hydrogen-bonded populations as high as ∼20%. These findings indicate that the polar nature of these residues may facilitate the transport of water molecules into the hydrophobic core of the membrane." @default.
- W2922580353 created "2019-04-01" @default.
- W2922580353 creator A5075162162 @default.
- W2922580353 creator A5078096234 @default.
- W2922580353 date "2019-05-01" @default.
- W2922580353 modified "2023-10-14" @default.
- W2922580353 title "Site-Specific Peptide Probes Detect Buried Water in a Lipid Membrane" @default.
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- W2922580353 doi "https://doi.org/10.1016/j.bpj.2019.03.002" @default.
- W2922580353 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6506627" @default.
- W2922580353 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31000156" @default.
- W2922580353 hasPublicationYear "2019" @default.
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