title: Mapping Hydration Dynamics around a β-Barrel Protein.
abstract: Protein surface hydration is fundamental to its structure, flexibility, dynamics, and function, but it has been challenging to disentangle their ultimate relationships. Here, we report our systematic characterization of hydration dynamics around a β-barrel protein, rat liver fatty acid-binding protein (rLFABP), to reveal the effect of different protein secondary structures on hydration water. We employed a tryptophan scan to the protein surface one at a time and examined a total of 17 different sites. We observed three types of hydration water relaxation with distinct time scales, from hundreds of femtoseconds to a hundred picoseconds. We also examined the anisotropy dynamics of the corresponding tryptophan side chains and observed two distinct relaxations from tens to hundreds of picoseconds. Integrating our previous findings on α-helical proteins, we conclude the following: (1) The hydration dynamics is highly heterogeneous around the protein surface of both α-helical and β-sheet proteins. The outer-layer water of the hydration shell behave like a bulk and relaxes in hundreds of femtoseconds. The inner-layer water collectively relaxes in two time scales, reorientation motions in a few picoseconds and network restructuring in tens to a hundred picoseconds. (2) The hydration dynamics are always faster than local protein relaxations and in fact drive the protein fluctuations on the picosecond time scale. (3) The hydration dynamics in general are more retarded around β-sheet structures than α-helical motifs. A thicker hydration shell and a more rigid interfacial hydration network are observed in the β-sheet protein. Overall, these findings elucidate the intimate relationship between water-protein interactions and dynamics on the ultrafast time scale.
authors.affiliation: Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Jin
authors.initials: J
authors.lastname: Yang
authors.affiliation: Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Yafang
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Lijuan
authors.initials: L
authors.lastname: Wang
authors.affiliation: Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
authors.forename: Dongping
authors.identifier: 0000-0001-9381-8992
authors.initials: D
authors.lastname: Zhong
mesh_terms: D000818:Animals; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017433:Protein Structure, Secondary; D051381:Rats; D013050:Spectrometry, Fluorescence; D014867:Water / Q000737:chemistry*
chemical_list: D050556:Fatty Acid-Binding Proteins; D014867:Water