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• W2016222666 abstract "The structure and dynamics of water around a protein is expected to be sensitive to the details of the adjacent secondary structure of the protein. In this article, we explore this sensitivity by calculating both the orientational dynamics of the surface water molecules and the equilibrium solvation time correlation function of the polar amino acid residues in each of the three helical segments of the protein HP-36, using atomistic molecular dynamics simulations. The solvation dynamics of polar amino acid residues in helix-2 is found to be faster than that of the other two helices (the average time constant is smaller by a factor of 2), although the interfacial water molecules around helix-2 exhibit much slower orientational dynamics than that around the other two helices. A careful analysis shows that the origin of such a counterintuitive behavior lies in the dependence of the solvation time correlation function on the surface exposure of the probethe more exposed is the probe, the faster the solvation dynamics. We discuss that these results are useful in explaining recent solvation dynamics experiments." @default.
• W2016222666 created "2016-06-24" @default.
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• W2016222666 creator A5091631394 @default.
• W2016222666 date "2005-02-23" @default.
• W2016222666 modified "2023-09-27" @default.
• W2016222666 title "Sensitivity of Polar Solvation Dynamics to the Secondary Structures of Aqueous Proteins and the Role of Surface Exposure of the Probe" @default.
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• W2016222666 doi "https://doi.org/10.1021/ja042847r" @default.
• W2016222666 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15771544" @default.
• W2016222666 hasPublicationYear "2005" @default.
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