ArticleBiophysical journal2008
Conformational changes in the N-terminal region of photoactive yellow protein: a time-resolved diffusion study.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- Effect of Hydrated Ionic Liquid on Photocycle and Dynamics of Photoactive Yellow Protein.Molecules (Basel, Switzerland) · 2021Article
- Combined probes of X-ray scattering and optical spectroscopy reveal how global conformational change is temporally and spatially linked to local structural perturbation in photoactive yellow protein.Physical chemistry chemical physics : PCCP · 2016Article
- Protein structural dynamics revealed by time-resolved X-ray solution scattering.Accounts of chemical research · 2015Article
- Light-induced conformational changes in full-length Arabidopsis thaliana cryptochrome.Journal of molecular biology · 2011Article
- Photoreactions of aureochrome-1.Biophysical journal · 2011Article
- Predicting the reaction coordinates of millisecond light-induced conformational changes in photoactive yellow protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
5 authors.
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Abstract
The kinetics of conformational change in the N-terminal region of photoactive yellow protein (PYP) was studied by the time-resolved diffusion measurement. The transient grating signal that represented the protein diffusion of the ground state and pB state depended on the observation time range. An analysis of the signal based on the time-dependent diffusion coefficient clearly showed that protein diffusion changed with a time constant of 170 micros, corresponding to the pR(2) --> pB' transition. Since a previous diffusion study of N-terminal truncated PYPs had revealed that the change in the diffusion coefficient reflected the unfolding of the alpha-helices in the N-terminal region of PYP, the results indicate that this unfolding took place at the same rate as the pR(2) --> pB' transition. This demonstrates that the response of the conformational change in the N-terminal region was quite fast, probably due to changes in a specific hydrogen-bonding network of this domain.
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