Поисковый запрос: (<.>K=conformation<.>) |
Общее количество найденных документов : 14
Показаны документы с 1 по 14 |
1.
| Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins/P. V. Natashin [et al.] // FEBS Journal, 2014. т.Vol. 281,N Is. 5.-С.1432-1445
|
2.
| Fluorescence lifetime components reveal kinetic intermediate states upon equilibrium denaturation of carbonic anhydrase II/E. V. Nemtseva [et al.] // METHODS AND APPLICATIONS IN FLUORESCENCE:IOP PUBLISHING LTD, 2018. т.Vol. 6,N Is. 1.- Ст.015006
|
3.
| Fluorescence of calcium-discharged obelin: The structure and molecular mechanism of emitter formation/F. N. Tomilin [et al.] // Doklady Biochemistry and Biophysics, 2008. т.Vol. 422,N Is. 1.-С.279-284
|
4.
| High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH/Z. .. Wawrzak [et al.] // PROTEINS-STRUCTURE FUNCTION AND GENETICS:WILEY-LISS, 1999. т.Vol. 35,N Is. 4.-С.425-439
|
5.
| Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive/V. N. Petushkov [et al.] // Biochemistry, 1996. т.Vol. 35,N Is. 37.-С.12086-12093
|
6.
| Ligand binding and conformational states of the photoprotein obelin/E. V. Eremeeva [et al.] // FEBS LETTERS:ELSEVIER SCIENCE BV, 2012. т.Vol. 586,N Is. 23.-С.4173-4179
|
7.
| Luminescence Activity Decreases When v-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein—A Theoretical and Experimental Study/B. -W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. -J. Liu // Photochemistry and Photobiology:Blackwell Publishing Inc., 2020
|
8.
| Luminescence Activity Decreases Whenv-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein-A Theoretical and Experimental Study/B. W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. J. Liu // PHOTOCHEMISTRY AND PHOTOBIOLOGY:WILEY, 2020
|
9.
| NAD(P)H:FMN-Oxidoreductase Functioning Under Macromolecular Crowding: In Vitro Modeling/A. E. Govorun, E. N. Esimbekova, V. A. Kratasyuk // Doklady Biochemistry and Biophysics:Pleiades Publishing, 2019. т.Vol. 486,N Is. 1.-С.213-215
|
10.
| Role of Hsp90 and ATP in modulating apyrase activity and firefly luciferase kinetics/M. A. Kirillova [et al.] // International Journal of Biological Macromolecules:Elsevier B.V., 2019. т.Vol. 131.-С.691-696
|
11.
| Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state/G. A. Stepanyuk [et al.] // BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS:ELSEVIER SCIENCE BV, 2013. т.Vol. 1834,N Is. 10.-С.2139-2146
|
12.
| The Effect of Osmolytes on the Bioluminescent Reaction of Bacteria: Structural and Dynamic Properties/L. A. Sukovatyi, A. E. Lisitsa, V. A. Kratasyuk, E. V. Nemtseva // Biophysics (Russian Federation):Pleiades journals, 2020. т.Vol. 65,N Is. 6.-С.966-971
|
13.
| The interaction of C-terminal Tyr208 and Tyr13 of the first alpha-helix ensures a closed conformation of ctenophore photoprotein berovin/L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:ROYAL SOC CHEMISTRY, 2020. т.Vol. 19,N Is. 3.-С.313-323
|
14.
| The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin/L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochemical and Photobiological Sciences, 2020. т.Vol. 19,N Is. 3.-С.313-323
|
|