High-Precision Megahertz-to-Terahertz Dielectric Spectroscopy of Protein Collective Motions and Hydration Dynamics

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dc.contributor.authorCharkhesht, Alien
dc.contributor.authorRegmi, Chola K.en
dc.contributor.authorMitchell-Koch, Katie R.en
dc.contributor.authorCheng, Shengfengen
dc.contributor.authorVinh, Nguyen Q.en
dc.contributor.departmentPhysicsen
dc.date.accessioned2019-02-04T14:15:48Zen
dc.date.available2019-02-04T14:15:48Zen
dc.date.issued2018-06-21en
dc.date.updated2019-02-04T14:15:47Zen
dc.description.abstractThe low-frequency collective vibrational modes in proteins as well as the protein-water interface have been suggested as dominant factors controlling the efficiency of biochemical reactions and biological energy transport. It is thus crucial to uncover the mystery of the hydration structure and dynamics as well as their coupling to collective motions of proteins in aqueous solutions. Here, we report dielectric properties of aqueous bovine serum albumin protein solutions as a model system using an extremely sensitive dielectric spectrometer with frequencies spanning from megahertz to terahertz. The dielectric relaxation spectra reveal several polarization mechanisms at the molecular level with different time constants and dielectric strengths, reflecting the complexity of protein-water interactions. Combining the effective-medium approximation and molecular dynamics simulations, we have determined collective vibrational modes at terahertz frequencies and the number of water molecules in the tightly bound and loosely bound hydration layers. High-precision measurements of the number of hydration water molecules indicate that the dynamical influence of proteins extends beyond the first solvation layer, to around 7 Å distance from the protein surface, with the largest slowdown arising from water molecules directly hydrogen-bonded to the protein. Our results reveal critical information of protein dynamics and protein-water interfaces, which determine biochemical functions and reactivity of proteins.en
dc.description.versionPublished versionen
dc.format.extentPages 6341-6350en
dc.format.extent10 page(s)en
dc.format.mediumPrint-Electronicen
dc.identifier.doihttps://doi.org/10.1021/acs.jpcb.8b02872en
dc.identifier.eissn1520-5207en
dc.identifier.issn1520-6106en
dc.identifier.issue24en
dc.identifier.orcidCheng, Shengfeng [0000-0002-6066-2968]en
dc.identifier.pmid29791154en
dc.identifier.urihttp://hdl.handle.net/10919/87423en
dc.identifier.volume122en
dc.languageEnglishen
dc.publisherAmerican Chemical Societyen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000436380000004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectScience & Technologyen
dc.subjectPhysical Sciencesen
dc.subjectChemistry, Physicalen
dc.subjectChemistryen
dc.subjectPUMP-PROBE SPECTROSCOPYen
dc.subjectMOLECULAR-DYNAMICSen
dc.subjectLIQUID WATERen
dc.subjectABSORPTION-SPECTROSCOPYen
dc.subjectMOSSBAUER-SPECTROSCOPYen
dc.subjectNEUTRON-SCATTERINGen
dc.subjectFREQUENCYen
dc.subjectTEMPERATUREen
dc.subjectRELAXATIONen
dc.subjectPRESSUREen
dc.subject03 Chemical Sciencesen
dc.subject09 Engineeringen
dc.subject02 Physical Sciencesen
dc.titleHigh-Precision Megahertz-to-Terahertz Dielectric Spectroscopy of Protein Collective Motions and Hydration Dynamicsen
dc.title.serialJournal of Physical Chemistry Ben
dc.typeArticle - Refereeden
dc.type.otherJournalen
pubs.organisational-group/Virginia Tech/Scienceen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Science/Physicsen
pubs.organisational-group/Virginia Tech/Science/COS T&R Facultyen

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