Far Infrared Sensing Of The Oxidation State Of Heme Proteins

dc.creatorChen, J. -Y.
dc.creatorCerne, J.
dc.creatorMarkelz, A. G.
dc.date2003-07-23
dc.date.accessioned2026-07-07T02:52:32Z
dc.date.available2026-07-07T02:52:32Z
dc.descriptionWe propose a biosensor based on the change of terahertz (THz) dielectric response when a biotarget binds to a probe. The feasibility of this biosensor is examined by studying the change of THz transmission for thin films of heme proteins myoglobin (Mb) and cytochrome C (CytC) as a function oxygen binding. We measure a strong increase in both the index and absorbance with oxygen binding for both Mb and CytC. The measured changes occur for both dried and samples hydrated at 80% r.h. suggesting that using terahertz time domain spectroscopy (TTDS) to monitor the transmitted terahertz pulse through a biomolecular probe thin film in ambient environmental conditions could be used to determine the presence of a biomolecular target.
dc.descriptionsingle pdf file containing figures, 4 pages
dc.identifierhttps://arxiv.org/abs/cond-mat/0307557
dc.identifierhttp://arxiv.org/abs/cond-mat/0307557
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/21872
dc.subjectSoft Condensed Matter
dc.subjectMaterials Science
dc.subjectQuantitative Biology
dc.titleFar Infrared Sensing Of The Oxidation State Of Heme Proteins
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