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| 001 | 850884 | ||
| 005 | 20240619092058.0 | ||
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| 100 | 1 | _ | |a Röllen, Katrin |0 P:(DE-Juel1)157880 |b 0 |u fzj |
| 245 | _ | _ | |a Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein |
| 260 | _ | _ | |a Lawrence, Kan. |c 2018 |b PLoS |
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| 520 | _ | _ | |a Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor. We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas putida in solution by using small-angle X-ray scattering (SAXS). SAXS experiments of the fully populated light- and dark-states under steady-state conditions revealed significant structural differences between the two states that are in agreement with the known structures determined by crystallography. We followed the transition from the light- to the dark-state by using SAXS measurements in real-time. A two-state model based on the light- and dark-state conformations could describe the measured time-course SAXS data with a relaxation time τREC of ~ 34 to 35 min being larger than the recovery time found with UV/vis spectroscopy. Unlike the flavin chromophore-based UV/vis method that is sensitive to the local chromophore environment in flavoproteins, SAXS-based assay depends on protein conformational changes and provides with an alternative to measure the recovery kinetics. |
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| 700 | 1 | _ | |a Batra-Safferling, Renu |0 P:(DE-Juel1)131950 |b 2 |e Corresponding author |u fzj |
| 700 | 1 | _ | |a Stadler, Andreas Maximilian |0 P:(DE-Juel1)140278 |b 3 |e Corresponding author |
| 773 | _ | _ | |a 10.1371/journal.pone.0200746 |g Vol. 13, no. 7, p. e0200746 - |0 PERI:(DE-600)2267670-3 |n 7 |p e0200746 |t PLoS one |v 13 |y 2018 |x 1932-6203 |
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