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dc.contributor.authorQiu, Junyien
dc.contributor.authorYang, Binen
dc.contributor.authorSushko, Oleksandren
dc.contributor.authorPikersgill, Richard W.en
dc.contributor.authorDonnan, Robert S.en
dc.date.accessioned2016-05-23T15:26:28Zen
dc.date.available2016-05-23T15:26:28Zen
dc.date.issued2014-12-08en
dc.identifier.citationQiu, J., Yang, B., Sushko, O., Pikersgill, R. W., & Donnan, R. S. (2015). Comparing Terahertz transmission response on pH-dependent apomyoglobin proteins dynamics with circular dichroism. RF and Wireless Technologies for Biomedical and Healthcare Applications (IMWS-Bio), 2014 IEEE MTT-S International Microwave Workshop. London, United Kingdom.en
dc.identifier.isbn9781479954452en
dc.identifier.doi10.1109/IMWS-BIO.2014.7032420en
dc.identifier.urihttp://hdl.handle.net/10034/610571en
dc.description© 20xx IEEE. Personal use of this material is permitted. Permission from IEEE must be obtained for all other uses, in any current or future media, including reprinting/republishing this material for advertising or promotional purposes, creating new collective works, for resale or redistribution to servers or lists, or reuse of any copyrighted component of this work in other works.en
dc.description.abstractTerahertz time domain spectroscopy (THz-TDS) was used to study the transmission responses of pH-dependent apomyoglobin (ApoMb) dissolved solutions in 0.2-2.2 THz frequency domain, the THz-TDS technique was also benchmarked against circular dichroism (CD) by studying pH-related folding states changes of ApoMb protein. Results revealed that differences of pH-dependent ApoMb/water dynamics can be detected directly by the THz refractive index spectrum, and these differences are further proved to be caused mainly the effect of protonation of water and possibly water response leaded by protein conformation change.
dc.language.isoenen
dc.publisherIEEEen
dc.relation.urlhttp://ieeexplore.ieee.org/xpl/articleDetails.jsp?arnumber=7032420en
dc.subjectTHz; biological Proteinsen
dc.titleComparing Terahertz transmission response on pH-dependent apomyoglobin proteins dynamics with circular dichroismen
dc.typeMeetings and Proceedingsen
dc.contributor.departmentUniversity of Chesteren
dc.identifier.journalRF and Wireless Technologies for Biomedical and Healthcare Applications (IMWS-Bio), 2014 IEEE MTT-S International Microwave Workshopen
dc.internal.reviewer-noteConferenceen
dc.date.accepted2000-01-01en
or.grant.openaccessNoen
rioxxterms.funderxxen
rioxxterms.identifier.projectxxen
rioxxterms.versionAMen
rioxxterms.licenseref.startdate2016-06-14en
html.description.abstractTerahertz time domain spectroscopy (THz-TDS) was used to study the transmission responses of pH-dependent apomyoglobin (ApoMb) dissolved solutions in 0.2-2.2 THz frequency domain, the THz-TDS technique was also benchmarked against circular dichroism (CD) by studying pH-related folding states changes of ApoMb protein. Results revealed that differences of pH-dependent ApoMb/water dynamics can be detected directly by the THz refractive index spectrum, and these differences are further proved to be caused mainly the effect of protonation of water and possibly water response leaded by protein conformation change.


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