| dc.identifier.uri | http://hdl.handle.net/11401/77093 | |
| dc.description.sponsorship | This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree. | en_US |
| dc.format | Monograph | |
| dc.format.medium | Electronic Resource | en_US |
| dc.language.iso | en_US | |
| dc.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
| dc.type | Dissertation | |
| dcterms.abstract | Femtosecond (fs) excitation of photoreceptors results in protein structural changes that occur on the microsecond to millisecond timescale or longer. It is thus of fundamental interest to understand how these fast timescale events dictate large scale protein dynamics that occur on much longer (106 orders of magnitude) timescales. AppA is a blue light using FAD (BLUF) protein which acts as a transcriptional antirepressor in Rhodobacter sphaeroides. The ultrafast photocycle and IR spectra are well characterized and involve a near instantaneous (<100 fs) response of the protein matrix that surrounds the chromophore. While there has been extensive study on the ultrafast time scales there has never been an observation of the kinetics of the light induced structural changes in the protein. Here we investigated the ultrafast (ps) to ms structural dynamics through transient IR. The data show that significant structural changes occur on the sub microsecond timescale following photoactivation. In addition our work has expanded to other BLUF proteins. BlsA is a BLUF protein found in the pathogenic bacterium Acinetobacter baumannii. Vibrational data together with homology modeling identify significant differences in β 5 strand caused by photoactivation, a region of BLUF photoreceptors proposed to be essential for signal modulation, that are unique for BlsA. In addition, the BLUF protein PixD, from Synechocystis, was characterized by transient IR, where photoexcitation results in radical pair formation, an event not observed in AppA. Transient IR also revealed that light state formation is complete within nanoseconds for PixD, suggesting a unique mechanism for single and multidomain BLUF systems. | |
| dcterms.available | 2017-09-20T16:51:56Z | |
| dcterms.contributor | Tonge, Peter | en_US |
| dcterms.contributor | London, Erwin | en_US |
| dcterms.contributor | Scharer, Orlando | en_US |
| dcterms.contributor | Bowen, Mark. | en_US |
| dcterms.creator | Brust, Richard James | |
| dcterms.dateAccepted | 2017-09-20T16:51:56Z | |
| dcterms.dateSubmitted | 2017-09-20T16:51:56Z | |
| dcterms.description | Department of Chemistry. | en_US |
| dcterms.extent | 254 pg. | en_US |
| dcterms.format | Application/PDF | en_US |
| dcterms.format | Monograph | |
| dcterms.identifier | http://hdl.handle.net/11401/77093 | |
| dcterms.issued | 2013-12-01 | |
| dcterms.language | en_US | |
| dcterms.provenance | Made available in DSpace on 2017-09-20T16:51:56Z (GMT). No. of bitstreams: 1
Brust_grad.sunysb_0771E_11534.pdf: 8996331 bytes, checksum: c0a0f90afbe136adca072fe933c23dc1 (MD5)
Previous issue date: 1 | en |
| dcterms.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
| dcterms.subject | AppA, BLUF, Infrared, Time resolved | |
| dcterms.subject | Chemistry | |
| dcterms.title | Molecular Movie Magic: Real-time Picosecond to Microsecond Structural Dynamics of Photoactive Flavoproteins | |
| dcterms.type | Dissertation | |
