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Статті в журналах з теми "Sdsl-Epr"
Braun, Theresa, Malte Drescher, and Daniel Summerer. "Expanding the Genetic Code for Site-Directed Spin-Labeling." International Journal of Molecular Sciences 20, no. 2 (January 16, 2019): 373. http://dx.doi.org/10.3390/ijms20020373.
Повний текст джерелаKlare, Johann P. "Site-directed spin labeling EPR spectroscopy in protein research." Biological Chemistry 394, no. 10 (October 1, 2013): 1281–300. http://dx.doi.org/10.1515/hsz-2013-0155.
Повний текст джерелаSahu, Indra D., and Gary A. Lorigan. "Site-Directed Spin Labeling EPR for Studying Membrane Proteins." BioMed Research International 2018 (2018): 1–13. http://dx.doi.org/10.1155/2018/3248289.
Повний текст джерелаEtienne, Emilien, Annalisa Pierro, Ketty C. Tamburrini, Alessio Bonucci, Elisabetta Mileo, Marlène Martinho, and Valérie Belle. "Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SimLabel." Molecules 28, no. 3 (January 31, 2023): 1348. http://dx.doi.org/10.3390/molecules28031348.
Повний текст джерелаWang, Yan, Venkatesan Kathiresan, Yaoyi Chen, Yanping Hu, Wei Jiang, Guangcan Bai, Guoquan Liu, Peter Z. Qin, and Xianyang Fang. "Posttranscriptional site-directed spin labeling of large RNAs with an unnatural base pair system under non-denaturing conditions." Chemical Science 11, no. 35 (2020): 9655–64. http://dx.doi.org/10.1039/d0sc01717e.
Повний текст джерелаBöhme, Sabine, Heinz-Jürgen Steinhoff, and Johann P. Klare. "Accessing the distance range of interest in biomolecules: Site-directed spin labeling and DEER spectroscopy." Spectroscopy 24, no. 3-4 (2010): 283–88. http://dx.doi.org/10.1155/2010/729060.
Повний текст джерелаTessmer, Maxx H., and Stefan Stoll. "chiLife: An open-source Python package for in silico spin labeling and integrative protein modeling." PLOS Computational Biology 19, no. 3 (March 31, 2023): e1010834. http://dx.doi.org/10.1371/journal.pcbi.1010834.
Повний текст джерелаRoser, P., M. J. Schmidt, M. Drescher, and D. Summerer. "Site-directed spin labeling of proteins for distance measurements in vitro and in cells." Organic & Biomolecular Chemistry 14, no. 24 (2016): 5468–76. http://dx.doi.org/10.1039/c6ob00473c.
Повний текст джерелаGeorgieva, Elka R. "Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function." Nanotechnology Reviews 6, no. 1 (February 1, 2017): 75–92. http://dx.doi.org/10.1515/ntrev-2016-0080.
Повний текст джерелаSahu, Indra D., and Gary A. Lorigan. "Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins." Biomolecules 10, no. 5 (May 13, 2020): 763. http://dx.doi.org/10.3390/biom10050763.
Повний текст джерелаДисертації з теми "Sdsl-Epr"
Pierro, Annalisa. "Protein structural dynamics in bacteria via nitroxide-based SDSL-EPR spectroscopy : from method improvements to in-cell studies." Electronic Thesis or Diss., Aix-Marseille, 2021. http://theses.univ-amu.fr.lama.univ-amu.fr/211116_PIERRO_290xrxu60ryzjfl293g970fjmdnl_TH%20(1).pdf.
Повний текст джерелаThe study of biomolecules in their native environment has been one of the main goals of structural biology in the last decade. As a result, we are assisting to a remarkable increase of new "in-cell" approaches, like Cryo-ET, FRET and NMR. Among these approaches, Site-Directed Spin Labeling (SDSL) coupled to Electron Paramagnetic Resonance (EPR) spectroscopy shows competitive and advantageous features to capture protein dynamics inside cells. In particular, nitroxide-based SDSL-EPR combines the advantages of high sensitivity and the lack of size constraints on the biomolecule of interest with the ability to capture protein structural transitions and interactions at physiological temperature. Despite the methodological advancements of the technique that have allowed the community to obtain increasingly relevant results, progresses still need to be done.In this work, the main limitation of nitroxide-based SDSL-EPR has been addressed. In the first time, we focused on the development of delivery methods to introduce the labeled protein in bacterial cells. Next, the stability of nitroxide labels in reducing environments and in-cell has been assessed, monitoring in parallel the viability of the cells during the EPR measurements. Thanks to the results achieved in this methodological part, we were able to study the structural dynamics of two flexible chaperone proteins directly in bacterial cells: NarJ from Escherichia coli and UreG from Sporosarcina pasteurii. Finally, to go further in understanding the impact of the cellular environment on the protein dynamics, the data obtained in cellular context were compared with those obtained in vitro or in a cell-mimicking environment
Ghimire, Harishchandra. "Structure, Dynamics, and Distance Measurements in Membrane Proteins and Peptides using EPR Spectroscopic Techniques." Miami University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=miami1291739688.
Повний текст джерелаDunkel, Sabrina. "Structure and function of Colicin A / Cai and PutP studied by site directed spin labeling EPR spectroscopy." Doctoral thesis, 2014. https://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2014112412937.
Повний текст джерелаDoebber, Meike Anne. "EPR Analysis of a Two-State Conformational Equilibrium in an N. pharaonis HAMP Domain - Activation/Deactivation of a Signaling Unit"." Doctoral thesis, 2009. https://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2009032018.
Повний текст джерелаKlose, Daniel. "Combining site-directed spin labeling EPR spectroscopy and biomolecular simulations to study conformation and dynamics of membrane proteins." Doctoral thesis, 2015. https://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2015012913034.
Повний текст джерелаЧастини книг з теми "Sdsl-Epr"
Dröden, J., and M. Drescher. "Studying Molecular Chaperones and Their Client Interactions by Nanometer Distance Restraints from Electron Paramagnetic Resonance Spectroscopy." In Biophysics of Molecular Chaperones, 217–41. Royal Society of Chemistry, 2023. http://dx.doi.org/10.1039/bk9781839165986-00217.
Повний текст джерела