| dc.contributor.author | Stubblefield, Jackson Reese | |
| dc.date.accessioned | 2017-10-10T20:57:15Z | |
| dc.date.available | 2017-10-10T20:57:15Z | |
| dc.date.issued | 2016-05-04 | |
| dc.identifier | oksd_stubblefield_HT_2016 | |
| dc.identifier.uri | https://hdl.handle.net/11244/52363 | |
| dc.description.abstract | Photoactive Yellow Protein (PYP) is considered to be a model chromophoric protein. The dynamics of its active site during photoisomerization are considered to be a novel effect which have been looked at by several research teams around the world. Our research group designed a new time-resolved experimental system using a tunable laser and Fourier-Transform Infrared (FTIR) system in tandem. With this new experimental design we were able to analyze the active site of a Photoactive Yellow Protein mutant, N43S, during its several stages of the protein functional dynamics. Our research sets a precedent for future experimental groups hoping to utilize rapid-scan FTIR techniques to analyze PYP or other, similar chromophoric proteins. | |
| dc.format | application/pdf | |
| dc.language | en_US | |
| dc.rights | Copyright is held by the author who has granted the Oklahoma State University Library the non-exclusive right to share this material in its institutional repository. Contact Digital Library Services at lib-dls@okstate.edu or 405-744-9161 for the permission policy on the use, reproduction or distribution of this material. | |
| dc.title | Structural dynamics of Photoactive Yellow Protein | |
| osu.filename | oksd_stubblefield_HT_2016.pdf | |
| osu.accesstype | Open Access | |
| dc.type.genre | Honors Thesis | |
| dc.type.material | Text | |
| dc.contributor.director | Xie, Aihua | |
| dc.contributor.facultyreader | Zhou, Donghua H. | |
| thesis.degree.discipline | Physics | |
| thesis.degree.grantor | Oklahoma State University | |
