This title appears in the Scientific Report :
2003
Please use the identifier:
http://dx.doi.org/10.1021/bi020577o in citations.
Please use the identifier: http://hdl.handle.net/2128/669 in citations.
Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion
Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion
The dynamics of the PYP photocycle have been studied using time-resolved optical rotatory dispersion (TRORD) spectroscopy in the visible and far-UV spectral regions to probe the changes in the chromophore configuration and the protein secondary structure, respectively. The changes in the secondary s...
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Personal Name(s): | Chen, E. |
---|---|
Gensch, T. / Gross, A. B. / Hendriks, J. / Hellingwerf, K. J. / Kliger, D. S. | |
Contributing Institute: |
Zelluläre Signalverarbeitung; IBI-1 |
Published in: | Biochemistry, 42 (2003) S. 2062 - 2071 |
Imprint: |
Columbus, Ohio
American Chemical Society
2003
|
Physical Description: |
2062 - 2071 |
DOI: |
10.1021/bi020577o |
PubMed ID: |
12590594 |
Document Type: |
Journal Article |
Research Program: |
Neurowissenschaften |
Series Title: |
Biochemistry
42 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/669 in citations.
The dynamics of the PYP photocycle have been studied using time-resolved optical rotatory dispersion (TRORD) spectroscopy in the visible and far-UV spectral regions to probe the changes in the chromophore configuration and the protein secondary structure, respectively. The changes in the secondary structure in PYP upon photoisomerization of the chromophore can be described by two exponential lifetimes of 2 +/- 0.8 and 650 +/- 100 ms that correspond to unfolding and refolding processes, respectively. The TRORD experiments that follow the dynamics of the chromophore report three exponential components, with lifetimes of 10 +/- 3 micros, 1.5 +/- 0.5 ms, and 515 +/- 110 ms. A comparison of the kinetic behaviors of the chromophore and protein shows that during the decay of pR(465) an initial relaxation that is localized to the chromophore hydrophobic pocket precedes the formation of the chromophore and protein structures found in pB(355). In contrast, the protein and chromophore processes occur with similar time constants during inactivation of the signaling state. |