Artigos de revistas sobre o tema "Sdsl-Epr"
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Braun, Theresa, Malte Drescher e Daniel Summerer. "Expanding the Genetic Code for Site-Directed Spin-Labeling". International Journal of Molecular Sciences 20, n.º 2 (16 de janeiro de 2019): 373. http://dx.doi.org/10.3390/ijms20020373.
Texto completo da fonteKlare, Johann P. "Site-directed spin labeling EPR spectroscopy in protein research". Biological Chemistry 394, n.º 10 (1 de outubro de 2013): 1281–300. http://dx.doi.org/10.1515/hsz-2013-0155.
Texto completo da fonteSahu, Indra D., e 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.
Texto completo da fonteEtienne, Emilien, Annalisa Pierro, Ketty C. Tamburrini, Alessio Bonucci, Elisabetta Mileo, Marlène Martinho e Valérie Belle. "Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SimLabel". Molecules 28, n.º 3 (31 de janeiro de 2023): 1348. http://dx.doi.org/10.3390/molecules28031348.
Texto completo da fonteWang, Yan, Venkatesan Kathiresan, Yaoyi Chen, Yanping Hu, Wei Jiang, Guangcan Bai, Guoquan Liu, Peter Z. Qin e Xianyang Fang. "Posttranscriptional site-directed spin labeling of large RNAs with an unnatural base pair system under non-denaturing conditions". Chemical Science 11, n.º 35 (2020): 9655–64. http://dx.doi.org/10.1039/d0sc01717e.
Texto completo da fonteBöhme, Sabine, Heinz-Jürgen Steinhoff e Johann P. Klare. "Accessing the distance range of interest in biomolecules: Site-directed spin labeling and DEER spectroscopy". Spectroscopy 24, n.º 3-4 (2010): 283–88. http://dx.doi.org/10.1155/2010/729060.
Texto completo da fonteTessmer, Maxx H., e Stefan Stoll. "chiLife: An open-source Python package for in silico spin labeling and integrative protein modeling". PLOS Computational Biology 19, n.º 3 (31 de março de 2023): e1010834. http://dx.doi.org/10.1371/journal.pcbi.1010834.
Texto completo da fonteRoser, P., M. J. Schmidt, M. Drescher e D. Summerer. "Site-directed spin labeling of proteins for distance measurements in vitro and in cells". Organic & Biomolecular Chemistry 14, n.º 24 (2016): 5468–76. http://dx.doi.org/10.1039/c6ob00473c.
Texto completo da fonteGeorgieva, Elka R. "Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function". Nanotechnology Reviews 6, n.º 1 (1 de fevereiro de 2017): 75–92. http://dx.doi.org/10.1515/ntrev-2016-0080.
Texto completo da fonteSahu, Indra D., e Gary A. Lorigan. "Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins". Biomolecules 10, n.º 5 (13 de maio de 2020): 763. http://dx.doi.org/10.3390/biom10050763.
Texto completo da fonteHirst, Stephanie, Nathan Alexander, Kristian Kaufmann, Hassane Mchaourab e Jens Meiler. "Rosettaepr: Developing Protein Structure Prediction Methods using Sparse SDSL-EPR Data". Biophysical Journal 98, n.º 3 (janeiro de 2010): 461a—462a. http://dx.doi.org/10.1016/j.bpj.2009.12.2508.
Texto completo da fonteDoni, Davide, Leonardo Passerini, Gérard Audran, Sylvain R. A. Marque, Marvin Schulz, Javier Santos, Paola Costantini, Marco Bortolus e 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, n.º 24 (17 de dezembro de 2020): 9619. http://dx.doi.org/10.3390/ijms21249619.
Texto completo da fonteRendon, Julia, Margot Di Cesare, Alexia Godet, Guillaume Gerbaud, Emilien Etienne, Vincent Chaptal, Pierre Falson et al. "Conformational dynamics of the ABC-transporter BmrA reveals by SDSL-EPR spectroscopy". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863 (setembro de 2022): 148732. http://dx.doi.org/10.1016/j.bbabio.2022.148732.
Texto completo da fontePirman, Natasha L., e Gail E. Fanucci. "Investigation of the Intrinsically Disordered Protein IA3 by Multiple SDSL-EPR Techniques". Biophysical Journal 98, n.º 3 (janeiro de 2010): 257a. http://dx.doi.org/10.1016/j.bpj.2009.12.1397.
Texto completo da fonteAziz, Atya, John F. Hess, Madhu S. Budamagunta, John C. Voss e Paul G. FitzGerald. "To Determine the Structure of Vimentin Head Domain Using SDSL-EPR Approach". Biophysical Journal 98, n.º 3 (janeiro de 2010): 558a. http://dx.doi.org/10.1016/j.bpj.2009.12.3021.
Texto completo da fonteSahu, Indra D., e Gary A. Lorigan. "Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques". Biophysica 1, n.º 2 (30 de março de 2021): 106–25. http://dx.doi.org/10.3390/biophysica1020009.
Texto completo da fonteCooke, James A., Jean Chamoun, Michael W. Howell, Paul M. Curmi, Peter G. Fajer e Louise J. Brown. "Structure and Dynamics of the Mobile Domain of Troponin I by SDSL-EPR". Biophysical Journal 98, n.º 3 (janeiro de 2010): 148a. http://dx.doi.org/10.1016/j.bpj.2009.12.798.
Texto completo da fonteStowe, Rebecca, Gunjan Dixit, Indra D. Sahu, Alison Bates, Carole Dabney-Smith e Gary A. Lorigan. "Protein protein interactions of KCNQ1 and KCNE1 observed via SDSL EPR line shape analysis". Biophysical Journal 121, n.º 3 (fevereiro de 2022): 241a. http://dx.doi.org/10.1016/j.bpj.2021.11.1548.
Texto completo da fontePan, Yanxiong, Hui Li, Qiaobin Li, Mary Lenertz, Isabelle Schuster, Drew Jordahl, Xiao Zhu, Bingcan Chen e Zhongyu Yang. "Protocol for resolving enzyme orientation and dynamics in advanced porous materials via SDSL-EPR". STAR Protocols 2, n.º 3 (setembro de 2021): 100676. http://dx.doi.org/10.1016/j.xpro.2021.100676.
Texto completo da fonteHoofnagle, Andrew N., James W. Stoner, Thomas Lee, Sandra S. Eaton e Natalie G. Ahn. "Phosphorylation-Dependent Changes in Structure and Dynamics in ERK2 Detected by SDSL and EPR". Biophysical Journal 86, n.º 1 (janeiro de 2004): 395–403. http://dx.doi.org/10.1016/s0006-3495(04)74115-6.
Texto completo da fonteTANG, Li, LinChao GUO, Hong XIAN, 可. 吴, Yu ZHOU, ZhangBao WU Ke CHEN, Peng CHEN et al. "Study on motional and conformational changes of BSA in solution using SDSL-EPR technique". Chinese Science Bulletin 55, n.º 14 (1 de maio de 2010): 1365–69. http://dx.doi.org/10.1360/972010-176.
Texto completo da fontePirman, Natasha L., Eugene Milshteyn, Luis Galiano, Justin C. Hewlett e Gail E. Fanucci. "Characterization of the disordered-to-α-helical transition of IA3 by SDSL-EPR spectroscopy". Protein Science 20, n.º 1 (23 de dezembro de 2010): 150–59. http://dx.doi.org/10.1002/pro.547.
Texto completo da fonteStowe, Rebecca, Gunjan Dixit, Indra D. Sahu e Gary A. Lorigan. "Protein-Protein Interactions of KCNQ1 and KCNE1 Observed via SDSL-EPR Line Shape Analysis". Biophysical Journal 118, n.º 3 (fevereiro de 2020): 264a. http://dx.doi.org/10.1016/j.bpj.2019.11.1528.
Texto completo da fonteKavalenka, Aleh, Iztok Urbančič, Valérie Belle, Sabrina Rouger, Stéphanie Costanzo, Sandra Kure, André Fournel, Sonia Longhi, Bruno Guigliarelli e Janez Strancar. "Conformational Analysis of the Partially Disordered Measles Virus NTAIL-XD Complex by SDSL EPR Spectroscopy". Biophysical Journal 98, n.º 6 (março de 2010): 1055–64. http://dx.doi.org/10.1016/j.bpj.2009.11.036.
Texto completo da fonteLerch, Michael, Carlos López e Wayne L. Hubbell. "Conformational Flexibility and Structure in High-Pressure Excited States of Apomyoglobin Revealed by SDSL-EPR". Biophysical Journal 106, n.º 2 (janeiro de 2014): 259a. http://dx.doi.org/10.1016/j.bpj.2013.11.1521.
Texto completo da fontePornthep Sompornpisut e 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, n.º 1 (9 de abril de 2020): 34–38. http://dx.doi.org/10.31580/sps.v2i1.1239.
Texto completo da fonteLe Breton, N., S. Longhi, A. Rockenbauer, B. Guigliarelli, S. R. A. Marque, V. Belle e 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, n.º 40 (2019): 22584–88. http://dx.doi.org/10.1039/c9cp04660g.
Texto completo da fonteJassoy, J. Jacques, Caspar A. Heubach, Tobias Hett, Frédéric Bernhard, Florian R. Haege, Gregor Hagelueken e Olav Schiemann. "Site Selective and Efficient Spin Labeling of Proteins with a Maleimide-Functionalized Trityl Radical for Pulsed Dipolar EPR Spectroscopy". Molecules 24, n.º 15 (27 de julho de 2019): 2735. http://dx.doi.org/10.3390/molecules24152735.
Texto completo da fonteGeorgieva, Ekaterina, Vasil Atanasov, Rositsa Kostandieva, Vanya Tsoneva, Mitko Mitev, Georgi Arabadzhiev, Yovcho Yovchev, Yanka Karamalakova e 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, n.º 6 (18 de março de 2023): 5807. http://dx.doi.org/10.3390/ijms24065807.
Texto completo da fonteHomchaudhuri, Lopamudra, Miguel De Avila, Stina B. Nilsson, Vladimir V. Bamm, Abdiwahab A. Musse, Graham S. T. Smith, George Harauz e Joan M. Boggs. "SDSL-EPR Study of a C-terminal Segment of Myelin Basic Protein in a Myelin Mimetic Environment". Biophysical Journal 98, n.º 3 (janeiro de 2010): 232a—233a. http://dx.doi.org/10.1016/j.bpj.2009.12.1258.
Texto completo da fonteWang, Changzhen, Juntao Yang, Yu Zhou, Jianbo Cong, Guofu Dong, Xiangjun Hu, Li Tang e Ke Wu. "Mobility Study of Individual Residue Sites in the Carbohydrate Recognition Domain of LSECtin Using SDSL–EPR Technique". Applied Biochemistry and Biotechnology 167, n.º 8 (19 de junho de 2012): 2295–304. http://dx.doi.org/10.1007/s12010-012-9766-9.
Texto completo da fonteNickolaus, Chen, Carolyn Vargas, Jörg Reichenwallner, Mohammed Chakour, Benjamin Selmke, Rusha Chakraborty, Raghavan Varadarajan, Sandro Keller e 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, n.º 9-10 (22 de setembro de 2020): 877–86. http://dx.doi.org/10.1007/s00723-020-01232-y.
Texto completo da fonteGeorgieva, Ekaterina, Yanka Karamalakova, Georgi Arabadzhiev, Vasil Atanasov, Rositsa Kostandieva, Mitko Mitev, Vanya Tsoneva, Yovcho Yovchev e Galina Nikolova. "Site-Directed Spin Labeling EPR Spectroscopy for Determination of Albumin Structural Damage and Hypoalbuminemia in Critical COVID-19". Antioxidants 11, n.º 12 (22 de novembro de 2022): 2311. http://dx.doi.org/10.3390/antiox11122311.
Texto completo da fonteLi, Hui, Yanxiong Pan, Zhongyu Yang, Jiajia Rao e 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 (março de 2021): 37–50. http://dx.doi.org/10.1016/j.tifs.2021.01.022.
Texto completo da fonteDoni, Davide, Marta Meggiolaro, Javier Santos, Gérard Audran, Sylvain R. A. Marque, Paola Costantini, Marco Bortolus e Donatella Carbonera. "A Combined Spectroscopic and In Silico Approach to Evaluate the Interaction of Human Frataxin with Mitochondrial Superoxide Dismutase". Biomedicines 9, n.º 12 (25 de novembro de 2021): 1763. http://dx.doi.org/10.3390/biomedicines9121763.
Texto completo da fontePistolesi, Sara, Elisa Ferro, Annalisa Santucci, Riccardo Basosi, Lorenza Trabalzini e 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, n.º 1 (agosto de 2006): 49–57. http://dx.doi.org/10.1016/j.bpc.2006.03.021.
Texto completo da fonteEhrenberger, Michelle A., Aleida Vieyra, Jackie M. Esquiaqui e 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, n.º 3 (agosto de 2019): 839–44. http://dx.doi.org/10.1016/j.bbrc.2019.06.105.
Texto completo da fonteCrouch, Catherine, Margaret Bost, Tae Kim, Bryan Green, D. Arbuckle, Carl Grossman e Kathleen Howard. "Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes". Membranes 8, n.º 4 (8 de novembro de 2018): 103. http://dx.doi.org/10.3390/membranes8040103.
Texto completo da fonteFischer, Axel W., David M. Anderson, Maxx H. Tessmer, Dara W. Frank, Jimmy B. Feix e 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, n.º 6 (27 de junho de 2017): 2977–84. http://dx.doi.org/10.1021/acsomega.7b00349.
Texto completo da fonteUeki, Shoji, e 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.
Texto completo da fonteAziz, Atya, John F. Hess, Madhu S. Budamagunta, John C. Voss, Alexandre P. Kuzin, Yuanpeng J. Huang, Rong Xiao, Gaetano T. Montelione, Paul G. FitzGerald e 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, n.º 34 (26 de junho de 2012): 28349–61. http://dx.doi.org/10.1074/jbc.m111.334011.
Texto completo da fonteMileo, Elisabetta, Emilien Etienne, Marlène Martinho, Régine Lebrun, Valérie Roubaud, Paul Tordo, Brigitte Gontero, Bruno Guigliarelli, Sylvain R. A. Marque e 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, n.º 6 (22 de maio de 2013): 1110–17. http://dx.doi.org/10.1021/bc4000542.
Texto completo da fonteFischer, Axel W., Enrica Bordignon, Stephanie Bleicken, Ana J. García-Sáez, Gunnar Jeschke e 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, n.º 1 (julho de 2016): 62–71. http://dx.doi.org/10.1016/j.jsb.2016.04.014.
Texto completo da fonteUeki, Shoji, Jun Abe, Yasunori Ohba e 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.
Texto completo da fonteZhao, Chenchao, Hiroaki Yamashita, Keisuke Ueda, Shoji Ueki e 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.
Texto completo da fonteChen, Mengzhen, Tamás Kálai, Duilio Cascio, Michael D. Bridges, Julian P. Whitelegge, Matthias Elgeti e Wayne L. Hubbell. "A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins". Applied Magnetic Resonance, 14 de outubro de 2023. http://dx.doi.org/10.1007/s00723-023-01618-8.
Texto completo da fonteRoopnarine, Osha, e 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 de outubro de 2023. http://dx.doi.org/10.1007/s00723-023-01623-x.
Texto completo da fonteFries, Sandra J., Theresa S. Braun, Christoph Globisch, Christine Peter, Malte Drescher e Elke Deuerling. "Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy". Scientific Reports 11, n.º 1 (21 de abril de 2021). http://dx.doi.org/10.1038/s41598-021-87847-y.
Texto completo da fonte"Recent Developments in Electron Paramagnetic Resonance for Spectroscopic Applications". Biointerface Research in Applied Chemistry 13, n.º 1 (24 de janeiro de 2022): 45. http://dx.doi.org/10.33263/briac131.045.
Texto completo da fonteBonucci, Alessio, Martina Palomino-Schätzlein, Paula Malo de Molina, Arantxa Arbe, Roberta Pierattelli, Bruno Rizzuti, Juan L. Iovanna e José L. Neira. "Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1". Frontiers in Molecular Biosciences 8 (5 de julho de 2021). http://dx.doi.org/10.3389/fmolb.2021.684622.
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