Far Infrared Sensing Of The Oxidation State Of Heme Proteins

Details Far Infrared Sensing Of The Oxidation State Of Heme Proteins Far Infrared Sensing Of The Oxidation State Of Heme Proteins

2003-07-23

arxiv.org/abs/cond-mat/0307557v1

Physics

Condensed Matter

Soft Condensed Matter

single pdf file containing figures, 4 pages

Scientific paper

We 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.

Affiliated with

Also associated with

No associations

Rating

Far Infrared Sensing Of The Oxidation State Of Heme Proteins does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Far Infrared Sensing Of The Oxidation State Of Heme Proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Far Infrared Sensing Of The Oxidation State Of Heme Proteins will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-165772