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dc.contributor.authorCharkhesht, Ali
dc.contributor.authorRegmi, Chola K.
dc.contributor.authorMitchell-Koch, Katie R.
dc.contributor.authorCheng, Shengfeng
dc.contributor.authorVinh, Nguyen Q.
dc.date.accessioned2019-02-04T14:15:48Z
dc.date.available2019-02-04T14:15:48Z
dc.date.issued2018-06-21
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/10919/87423
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.
dc.format.extentPages 6341-6350
dc.format.extent10 page(s)
dc.format.mediumPrint-Electronic
dc.languageEnglish
dc.publisherAMER CHEMICAL SOC
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=930d57c9ac61a043676db62af60056c1
dc.rightsIn Copyright (InC)
dc.rightsThis Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subjectScience & Technology
dc.subjectPhysical Sciences
dc.subjectChemistry, Physical
dc.subjectChemistry
dc.subjectPUMP-PROBE SPECTROSCOPY
dc.subjectMOLECULAR-DYNAMICS
dc.subjectLIQUID WATER
dc.subjectABSORPTION-SPECTROSCOPY
dc.subjectMOSSBAUER-SPECTROSCOPY
dc.subjectNEUTRON-SCATTERING
dc.subjectFREQUENCY
dc.subjectTEMPERATURE
dc.subjectRELAXATION
dc.subjectPRESSURE
dc.subject03 Chemical Sciences
dc.subject09 Engineering
dc.subject02 Physical Sciences
dc.titleHigh-Precision Megahertz-to-Terahertz Dielectric Spectroscopy of Protein Collective Motions and Hydration Dynamics
dc.typeArticle - Refereed
dc.date.updated2019-02-04T14:15:47Z
dc.description.versionPublished (Publication status)
dc.title.serialJOURNAL OF PHYSICAL CHEMISTRY B
dc.identifier.doihttps://doi.org/10.1021/acs.jpcb.8b02872
dc.type.otherJournal
dc.identifier.volume122
dc.identifier.issue24
dc.identifier.orcidCheng, Shengfeng [0000-0002-6066-2968]
dc.identifier.pmid29791154
dc.identifier.eissn1520-5207
pubs.organisational-group/Virginia Tech/Science
pubs.organisational-group/Virginia Tech
pubs.organisational-group/Virginia Tech/All T&R Faculty
pubs.organisational-group/Virginia Tech/Science/Physics
pubs.organisational-group/Virginia Tech/Science/COS T&R Faculty


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