Artykuły w czasopismach na temat „Sdsl-Epr”
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Braun, Theresa, Malte Drescher i Daniel Summerer. "Expanding the Genetic Code for Site-Directed Spin-Labeling". International Journal of Molecular Sciences 20, nr 2 (16.01.2019): 373. http://dx.doi.org/10.3390/ijms20020373.
Pełny tekst źródłaKlare, Johann P. "Site-directed spin labeling EPR spectroscopy in protein research". Biological Chemistry 394, nr 10 (1.10.2013): 1281–300. http://dx.doi.org/10.1515/hsz-2013-0155.
Pełny tekst źródłaSahu, Indra D., i 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.
Pełny tekst źródłaEtienne, Emilien, Annalisa Pierro, Ketty C. Tamburrini, Alessio Bonucci, Elisabetta Mileo, Marlène Martinho i Valérie Belle. "Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SimLabel". Molecules 28, nr 3 (31.01.2023): 1348. http://dx.doi.org/10.3390/molecules28031348.
Pełny tekst źródłaWang, Yan, Venkatesan Kathiresan, Yaoyi Chen, Yanping Hu, Wei Jiang, Guangcan Bai, Guoquan Liu, Peter Z. Qin i Xianyang Fang. "Posttranscriptional site-directed spin labeling of large RNAs with an unnatural base pair system under non-denaturing conditions". Chemical Science 11, nr 35 (2020): 9655–64. http://dx.doi.org/10.1039/d0sc01717e.
Pełny tekst źródłaBöhme, Sabine, Heinz-Jürgen Steinhoff i Johann P. Klare. "Accessing the distance range of interest in biomolecules: Site-directed spin labeling and DEER spectroscopy". Spectroscopy 24, nr 3-4 (2010): 283–88. http://dx.doi.org/10.1155/2010/729060.
Pełny tekst źródłaTessmer, Maxx H., i Stefan Stoll. "chiLife: An open-source Python package for in silico spin labeling and integrative protein modeling". PLOS Computational Biology 19, nr 3 (31.03.2023): e1010834. http://dx.doi.org/10.1371/journal.pcbi.1010834.
Pełny tekst źródłaRoser, P., M. J. Schmidt, M. Drescher i D. Summerer. "Site-directed spin labeling of proteins for distance measurements in vitro and in cells". Organic & Biomolecular Chemistry 14, nr 24 (2016): 5468–76. http://dx.doi.org/10.1039/c6ob00473c.
Pełny tekst źródłaGeorgieva, Elka R. "Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function". Nanotechnology Reviews 6, nr 1 (1.02.2017): 75–92. http://dx.doi.org/10.1515/ntrev-2016-0080.
Pełny tekst źródłaSahu, Indra D., i Gary A. Lorigan. "Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins". Biomolecules 10, nr 5 (13.05.2020): 763. http://dx.doi.org/10.3390/biom10050763.
Pełny tekst źródłaHirst, Stephanie, Nathan Alexander, Kristian Kaufmann, Hassane Mchaourab i Jens Meiler. "Rosettaepr: Developing Protein Structure Prediction Methods using Sparse SDSL-EPR Data". Biophysical Journal 98, nr 3 (styczeń 2010): 461a—462a. http://dx.doi.org/10.1016/j.bpj.2009.12.2508.
Pełny tekst źródłaDoni, Davide, Leonardo Passerini, Gérard Audran, Sylvain R. A. Marque, Marvin Schulz, Javier Santos, Paola Costantini, Marco Bortolus i Donatella Carbonera. "Effects of Fe2+/Fe3+ Binding to Human Frataxin and Its D122Y Variant, as Revealed by Site-Directed Spin Labeling (SDSL) EPR Complemented by Fluorescence and Circular Dichroism Spectroscopies". International Journal of Molecular Sciences 21, nr 24 (17.12.2020): 9619. http://dx.doi.org/10.3390/ijms21249619.
Pełny tekst źródłaRendon, Julia, Margot Di Cesare, Alexia Godet, Guillaume Gerbaud, Emilien Etienne, Vincent Chaptal, Pierre Falson i in. "Conformational dynamics of the ABC-transporter BmrA reveals by SDSL-EPR spectroscopy". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863 (wrzesień 2022): 148732. http://dx.doi.org/10.1016/j.bbabio.2022.148732.
Pełny tekst źródłaPirman, Natasha L., i Gail E. Fanucci. "Investigation of the Intrinsically Disordered Protein IA3 by Multiple SDSL-EPR Techniques". Biophysical Journal 98, nr 3 (styczeń 2010): 257a. http://dx.doi.org/10.1016/j.bpj.2009.12.1397.
Pełny tekst źródłaAziz, Atya, John F. Hess, Madhu S. Budamagunta, John C. Voss i Paul G. FitzGerald. "To Determine the Structure of Vimentin Head Domain Using SDSL-EPR Approach". Biophysical Journal 98, nr 3 (styczeń 2010): 558a. http://dx.doi.org/10.1016/j.bpj.2009.12.3021.
Pełny tekst źródłaSahu, Indra D., i Gary A. Lorigan. "Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques". Biophysica 1, nr 2 (30.03.2021): 106–25. http://dx.doi.org/10.3390/biophysica1020009.
Pełny tekst źródłaCooke, James A., Jean Chamoun, Michael W. Howell, Paul M. Curmi, Peter G. Fajer i Louise J. Brown. "Structure and Dynamics of the Mobile Domain of Troponin I by SDSL-EPR". Biophysical Journal 98, nr 3 (styczeń 2010): 148a. http://dx.doi.org/10.1016/j.bpj.2009.12.798.
Pełny tekst źródłaStowe, Rebecca, Gunjan Dixit, Indra D. Sahu, Alison Bates, Carole Dabney-Smith i Gary A. Lorigan. "Protein protein interactions of KCNQ1 and KCNE1 observed via SDSL EPR line shape analysis". Biophysical Journal 121, nr 3 (luty 2022): 241a. http://dx.doi.org/10.1016/j.bpj.2021.11.1548.
Pełny tekst źródłaPan, Yanxiong, Hui Li, Qiaobin Li, Mary Lenertz, Isabelle Schuster, Drew Jordahl, Xiao Zhu, Bingcan Chen i Zhongyu Yang. "Protocol for resolving enzyme orientation and dynamics in advanced porous materials via SDSL-EPR". STAR Protocols 2, nr 3 (wrzesień 2021): 100676. http://dx.doi.org/10.1016/j.xpro.2021.100676.
Pełny tekst źródłaHoofnagle, Andrew N., James W. Stoner, Thomas Lee, Sandra S. Eaton i Natalie G. Ahn. "Phosphorylation-Dependent Changes in Structure and Dynamics in ERK2 Detected by SDSL and EPR". Biophysical Journal 86, nr 1 (styczeń 2004): 395–403. http://dx.doi.org/10.1016/s0006-3495(04)74115-6.
Pełny tekst źródłaTANG, Li, LinChao GUO, Hong XIAN, 可. 吴, Yu ZHOU, ZhangBao WU Ke CHEN, Peng CHEN i in. "Study on motional and conformational changes of BSA in solution using SDSL-EPR technique". Chinese Science Bulletin 55, nr 14 (1.05.2010): 1365–69. http://dx.doi.org/10.1360/972010-176.
Pełny tekst źródłaPirman, Natasha L., Eugene Milshteyn, Luis Galiano, Justin C. Hewlett i Gail E. Fanucci. "Characterization of the disordered-to-α-helical transition of IA3 by SDSL-EPR spectroscopy". Protein Science 20, nr 1 (23.12.2010): 150–59. http://dx.doi.org/10.1002/pro.547.
Pełny tekst źródłaStowe, Rebecca, Gunjan Dixit, Indra D. Sahu i Gary A. Lorigan. "Protein-Protein Interactions of KCNQ1 and KCNE1 Observed via SDSL-EPR Line Shape Analysis". Biophysical Journal 118, nr 3 (luty 2020): 264a. http://dx.doi.org/10.1016/j.bpj.2019.11.1528.
Pełny tekst źródłaKavalenka, Aleh, Iztok Urbančič, Valérie Belle, Sabrina Rouger, Stéphanie Costanzo, Sandra Kure, André Fournel, Sonia Longhi, Bruno Guigliarelli i Janez Strancar. "Conformational Analysis of the Partially Disordered Measles Virus NTAIL-XD Complex by SDSL EPR Spectroscopy". Biophysical Journal 98, nr 6 (marzec 2010): 1055–64. http://dx.doi.org/10.1016/j.bpj.2009.11.036.
Pełny tekst źródłaLerch, Michael, Carlos López i Wayne L. Hubbell. "Conformational Flexibility and Structure in High-Pressure Excited States of Apomyoglobin Revealed by SDSL-EPR". Biophysical Journal 106, nr 2 (styczeń 2014): 259a. http://dx.doi.org/10.1016/j.bpj.2013.11.1521.
Pełny tekst źródłaPornthep Sompornpisut i Ngoc Lan Le Nguyen. "Structure and dynamics of spin label side chains in KvAP voltage-sensor domain: an all-atom MD simulation study". Science Proceedings Series 2, nr 1 (9.04.2020): 34–38. http://dx.doi.org/10.31580/sps.v2i1.1239.
Pełny tekst źródłaLe Breton, N., S. Longhi, A. Rockenbauer, B. Guigliarelli, S. R. A. Marque, V. Belle i M. Martinho. "Probing the dynamic properties of two sites simultaneously in a protein–protein interaction process: a SDSL-EPR study". Physical Chemistry Chemical Physics 21, nr 40 (2019): 22584–88. http://dx.doi.org/10.1039/c9cp04660g.
Pełny tekst źródłaJassoy, J. Jacques, Caspar A. Heubach, Tobias Hett, Frédéric Bernhard, Florian R. Haege, Gregor Hagelueken i Olav Schiemann. "Site Selective and Efficient Spin Labeling of Proteins with a Maleimide-Functionalized Trityl Radical for Pulsed Dipolar EPR Spectroscopy". Molecules 24, nr 15 (27.07.2019): 2735. http://dx.doi.org/10.3390/molecules24152735.
Pełny tekst źródłaGeorgieva, Ekaterina, Vasil Atanasov, Rositsa Kostandieva, Vanya Tsoneva, Mitko Mitev, Georgi Arabadzhiev, Yovcho Yovchev, Yanka Karamalakova i Galina Nikolova. "Direct Application of 3-Maleimido-PROXYL for Proving Hypoalbuminemia in Cases of SARS-CoV-2 Infection: The Potential Diagnostic Method of Determining Albumin Instability and Oxidized Protein Level in Severe COVID-19". International Journal of Molecular Sciences 24, nr 6 (18.03.2023): 5807. http://dx.doi.org/10.3390/ijms24065807.
Pełny tekst źródłaHomchaudhuri, Lopamudra, Miguel De Avila, Stina B. Nilsson, Vladimir V. Bamm, Abdiwahab A. Musse, Graham S. T. Smith, George Harauz i Joan M. Boggs. "SDSL-EPR Study of a C-terminal Segment of Myelin Basic Protein in a Myelin Mimetic Environment". Biophysical Journal 98, nr 3 (styczeń 2010): 232a—233a. http://dx.doi.org/10.1016/j.bpj.2009.12.1258.
Pełny tekst źródłaWang, Changzhen, Juntao Yang, Yu Zhou, Jianbo Cong, Guofu Dong, Xiangjun Hu, Li Tang i Ke Wu. "Mobility Study of Individual Residue Sites in the Carbohydrate Recognition Domain of LSECtin Using SDSL–EPR Technique". Applied Biochemistry and Biotechnology 167, nr 8 (19.06.2012): 2295–304. http://dx.doi.org/10.1007/s12010-012-9766-9.
Pełny tekst źródłaNickolaus, Chen, Carolyn Vargas, Jörg Reichenwallner, Mohammed Chakour, Benjamin Selmke, Rusha Chakraborty, Raghavan Varadarajan, Sandro Keller i Wolfgang E. Trommer. "The Molten Globule State of Maltose-Binding Protein: Structural and Thermodynamic Characterization by EPR Spectroscopy and Isothermal Titration Calorimetry". Applied Magnetic Resonance 51, nr 9-10 (22.09.2020): 877–86. http://dx.doi.org/10.1007/s00723-020-01232-y.
Pełny tekst źródłaGeorgieva, Ekaterina, Yanka Karamalakova, Georgi Arabadzhiev, Vasil Atanasov, Rositsa Kostandieva, Mitko Mitev, Vanya Tsoneva, Yovcho Yovchev i Galina Nikolova. "Site-Directed Spin Labeling EPR Spectroscopy for Determination of Albumin Structural Damage and Hypoalbuminemia in Critical COVID-19". Antioxidants 11, nr 12 (22.11.2022): 2311. http://dx.doi.org/10.3390/antiox11122311.
Pełny tekst źródłaLi, Hui, Yanxiong Pan, Zhongyu Yang, Jiajia Rao i Bingcan Chen. "Emerging applications of site-directed spin labeling electron paramagnetic resonance (SDSL-EPR) to study food protein structure, dynamics, and interaction". Trends in Food Science & Technology 109 (marzec 2021): 37–50. http://dx.doi.org/10.1016/j.tifs.2021.01.022.
Pełny tekst źródłaDoni, Davide, Marta Meggiolaro, Javier Santos, Gérard Audran, Sylvain R. A. Marque, Paola Costantini, Marco Bortolus i Donatella Carbonera. "A Combined Spectroscopic and In Silico Approach to Evaluate the Interaction of Human Frataxin with Mitochondrial Superoxide Dismutase". Biomedicines 9, nr 12 (25.11.2021): 1763. http://dx.doi.org/10.3390/biomedicines9121763.
Pełny tekst źródłaPistolesi, Sara, Elisa Ferro, Annalisa Santucci, Riccardo Basosi, Lorenza Trabalzini i Rebecca Pogni. "Molecular motion of spin labeled side chains in the C-terminal domain of RGL2 protein: A SDSL-EPR and MD study". Biophysical Chemistry 123, nr 1 (sierpień 2006): 49–57. http://dx.doi.org/10.1016/j.bpc.2006.03.021.
Pełny tekst źródłaEhrenberger, Michelle A., Aleida Vieyra, Jackie M. Esquiaqui i Gail E. Fanucci. "Ion-dependent mobility effects of the Fusobacterium nucleatum glycine riboswitch aptamer II via site-directed spin-labeling (SDSL) electron paramagnetic resonance (EPR)". Biochemical and Biophysical Research Communications 516, nr 3 (sierpień 2019): 839–44. http://dx.doi.org/10.1016/j.bbrc.2019.06.105.
Pełny tekst źródłaCrouch, Catherine, Margaret Bost, Tae Kim, Bryan Green, D. Arbuckle, Carl Grossman i Kathleen Howard. "Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes". Membranes 8, nr 4 (8.11.2018): 103. http://dx.doi.org/10.3390/membranes8040103.
Pełny tekst źródłaFischer, Axel W., David M. Anderson, Maxx H. Tessmer, Dara W. Frank, Jimmy B. Feix i Jens Meiler. "Structure and Dynamics of Type III Secretion Effector Protein ExoU As determined by SDSL-EPR Spectroscopy in Conjunction with De Novo Protein Folding". ACS Omega 2, nr 6 (27.06.2017): 2977–84. http://dx.doi.org/10.1021/acsomega.7b00349.
Pełny tekst źródłaUeki, Shoji, i Toshiaki Arata. "1P154 SDSL-EPR study of the effect of troponin I phosphorylation on the structure of cardiac troponin C(Muscle-muscle proteins and contraction,Oral Presentations)". Seibutsu Butsuri 47, supplement (2007): S62. http://dx.doi.org/10.2142/biophys.47.s62_1.
Pełny tekst źródłaAziz, Atya, John F. Hess, Madhu S. Budamagunta, John C. Voss, Alexandre P. Kuzin, Yuanpeng J. Huang, Rong Xiao, Gaetano T. Montelione, Paul G. FitzGerald i John F. Hunt. "The Structure of Vimentin Linker 1 and Rod 1B Domains Characterized by Site-directed Spin-labeling Electron Paramagnetic Resonance (SDSL-EPR) and X-ray Crystallography". Journal of Biological Chemistry 287, nr 34 (26.06.2012): 28349–61. http://dx.doi.org/10.1074/jbc.m111.334011.
Pełny tekst źródłaMileo, Elisabetta, Emilien Etienne, Marlène Martinho, Régine Lebrun, Valérie Roubaud, Paul Tordo, Brigitte Gontero, Bruno Guigliarelli, Sylvain R. A. Marque i Valérie Belle. "Enlarging the Panoply of Site-Directed Spin Labeling Electron Paramagnetic Resonance (SDSL-EPR): Sensitive and Selective Spin-Labeling of Tyrosine Using an Isoindoline-Based Nitroxide". Bioconjugate Chemistry 24, nr 6 (22.05.2013): 1110–17. http://dx.doi.org/10.1021/bc4000542.
Pełny tekst źródłaFischer, Axel W., Enrica Bordignon, Stephanie Bleicken, Ana J. García-Sáez, Gunnar Jeschke i Jens Meiler. "Pushing the size limit of de novo structure ensemble prediction guided by sparse SDSL-EPR restraints to 200 residues: The monomeric and homodimeric forms of BAX". Journal of Structural Biology 195, nr 1 (lipiec 2016): 62–71. http://dx.doi.org/10.1016/j.jsb.2016.04.014.
Pełny tekst źródłaUeki, Shoji, Jun Abe, Yasunori Ohba i Toshiaki Arata. "3P-003 The influence of the spin label mobility on the distance measurement of SDSL EPR in protein structure(Protein:Structure,The 47th Annual Meeting of the Biophysical Society of Japan)". Seibutsu Butsuri 49, supplement (2009): S151. http://dx.doi.org/10.2142/biophys.49.s151_2.
Pełny tekst źródłaZhao, Chenchao, Hiroaki Yamashita, Keisuke Ueda, Shoji Ueki i Toshiaki Arata. "1P143 Structural Dynamics of N-terminal Extension of Cardiac Troponin I by Site Directed Spin Labeling-EPR(10.Muscle,Poster,The 51st Annual Meeting of the Biophysical Society of Japan)". Seibutsu Butsuri 53, supplement1-2 (2013): S129. http://dx.doi.org/10.2142/biophys.53.s129_4.
Pełny tekst źródłaChen, Mengzhen, Tamás Kálai, Duilio Cascio, Michael D. Bridges, Julian P. Whitelegge, Matthias Elgeti i Wayne L. Hubbell. "A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins". Applied Magnetic Resonance, 14.10.2023. http://dx.doi.org/10.1007/s00723-023-01618-8.
Pełny tekst źródłaRoopnarine, Osha, i David D. Thomas. "Structural Dynamics of Protein Interactions Using Site-Directed Spin Labeling of Cysteines to Measure Distances and Rotational Dynamics with EPR Spectroscopy". Applied Magnetic Resonance, 11.10.2023. http://dx.doi.org/10.1007/s00723-023-01623-x.
Pełny tekst źródłaFries, Sandra J., Theresa S. Braun, Christoph Globisch, Christine Peter, Malte Drescher i Elke Deuerling. "Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy". Scientific Reports 11, nr 1 (21.04.2021). http://dx.doi.org/10.1038/s41598-021-87847-y.
Pełny tekst źródła"Recent Developments in Electron Paramagnetic Resonance for Spectroscopic Applications". Biointerface Research in Applied Chemistry 13, nr 1 (24.01.2022): 45. http://dx.doi.org/10.33263/briac131.045.
Pełny tekst źródłaBonucci, Alessio, Martina Palomino-Schätzlein, Paula Malo de Molina, Arantxa Arbe, Roberta Pierattelli, Bruno Rizzuti, Juan L. Iovanna i José L. Neira. "Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1". Frontiers in Molecular Biosciences 8 (5.07.2021). http://dx.doi.org/10.3389/fmolb.2021.684622.
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