Добірка наукової літератури з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
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Статті в журналах з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
Yang, Ziyu, Haiqi Xu, Jiayu Wang, Wei Chen, and Meiping Zhao. "Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis." Applied Spectroscopy 75, no. 5 (April 20, 2021): 491–505. http://dx.doi.org/10.1177/00037028211009973.
Повний текст джерелаSengupta, Bhaswati, and Mai Huynh. "Contribution of smFRET to Chromatin Research." Biophysica 3, no. 1 (February 8, 2023): 93–108. http://dx.doi.org/10.3390/biophysica3010007.
Повний текст джерелаLeBlanc, Sharonda, Prakash Kulkarni, and Keith Weninger. "Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins." Biomolecules 8, no. 4 (November 8, 2018): 140. http://dx.doi.org/10.3390/biom8040140.
Повний текст джерелаLi, Maodong, Tanlin Sun, Fan Jin, Daqi Yu, and Zhirong Liu. "Dimension conversion and scaling of disordered protein chains." Molecular BioSystems 12, no. 9 (2016): 2932–40. http://dx.doi.org/10.1039/c6mb00415f.
Повний текст джерелаYukhnovets, Olessya, Henning Höfig, Nuno Bustorff, Alexandros Katranidis, and Jörg Fitter. "Impact of Molecule Concentration, Diffusion Rates and Surface Passivation on Single-Molecule Fluorescence Studies in Solution." Biomolecules 12, no. 3 (March 18, 2022): 468. http://dx.doi.org/10.3390/biom12030468.
Повний текст джерелаHu, Jinyong, Meiyan Wu, Li Jiang, Zhensheng Zhong, Zhangkai Zhou, Thitima Rujiralai, and Jie Ma. "Combining gold nanoparticle antennas with single-molecule fluorescence resonance energy transfer (smFRET) to study DNA hairpin dynamics." Nanoscale 10, no. 14 (2018): 6611–19. http://dx.doi.org/10.1039/c7nr08397a.
Повний текст джерелаGirodat, Dylan, Avik K. Pati, Daniel S. Terry, Scott C. Blanchard, and Karissa Y. Sanbonmatsu. "Quantitative comparison between sub-millisecond time resolution single-molecule FRET measurements and 10-second molecular simulations of a biosensor protein." PLOS Computational Biology 16, no. 11 (November 5, 2020): e1008293. http://dx.doi.org/10.1371/journal.pcbi.1008293.
Повний текст джерелаYang, Jie, Sarah Perrett, and Si Wu. "Single Molecule Characterization of Amyloid Oligomers." Molecules 26, no. 4 (February 11, 2021): 948. http://dx.doi.org/10.3390/molecules26040948.
Повний текст джерелаVerma, Awadhesh Kumar, Ashab Noumani, Amit K. Yadav, and Pratima R. Solanki. "FRET Based Biosensor: Principle Applications Recent Advances and Challenges." Diagnostics 13, no. 8 (April 8, 2023): 1375. http://dx.doi.org/10.3390/diagnostics13081375.
Повний текст джерелаDurham, Ryan J., Nabina Paudyal, Elisa Carrillo, Nidhi Kaur Bhatia, David M. Maclean, Vladimir Berka, Drew M. Dolino, Alemayehu A. Gorfe, and Vasanthi Jayaraman. "Conformational spread and dynamics in allostery of NMDA receptors." Proceedings of the National Academy of Sciences 117, no. 7 (February 3, 2020): 3839–47. http://dx.doi.org/10.1073/pnas.1910950117.
Повний текст джерелаДисертації з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
Wallace, Mark Ian. "A study of DNA conformational dynamics using single-molecule fluorescence resonance energy transfer." Thesis, University of Cambridge, 2001. https://www.repository.cam.ac.uk/handle/1810/251799.
Повний текст джерелаSchuler, Benjamin, Everett A. Lipman, Peter J. Steinbach, Michael Kumke, and William A. Eaton. "Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence." Universität Potsdam, 2005. http://opus.kobv.de/ubp/volltexte/2007/1222/.
Повний текст джерелаUphoff, Stephan. "Studying protein-DNA interactions in vitro and in vivo using single-molecule photoswitching." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:d0a52864-6d26-44a4-8fb7-5d12624a04ba.
Повний текст джерелаBrehove, Matthew Steven. "Access to the Genome: A Study of Transcription Factor Binding Within Nucleosomes." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1480603783786784.
Повний текст джерелаPérez, González Daniel Cibrán. "Single-molecule studies of nucleic acid folding and nucleic acid-protein interactions." Thesis, University of St Andrews, 2017. http://hdl.handle.net/10023/12039.
Повний текст джерелаQureshi, Mohammad Haroon. "Replication Protein A Mediated G-Quadruplex Unfolding - A Single Molecule FRET Study." Kent State University / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=kent1385984615.
Повний текст джерелаHwang, William Liang. "The Mechanism and Regulation of Chromatin Remodeling by ISWI Family Enzymes." Thesis, Harvard University, 2013. http://dissertations.umi.com/gsas.harvard:10947.
Повний текст джерелаPiguet, Joachim. "Advanced Fluorescence Microscopy to Study Plasma Membrane Protein Dynamics." Doctoral thesis, Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-178147.
Повний текст джерелаQC 20151217
Valeri, Alessandro [Verfasser]. "Fluorescence resonance energy transfer between multiple chromophores studied by single-molecule spectroscopy / Alessandro Valeri." 2010. http://d-nb.info/1000132781/34.
Повний текст джерелаHuang, Yun-Tzu, and 黃蘊慈. "Distance Variations between Active Sites of H+-pyrophosphatase Determined by Single Molecule Fluorescence Resonance Energy Transfer." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/86183766690838245647.
Повний текст джерела國立清華大學
生物資訊與結構生物研究所
98
Homodimeric H+-pyrophosphatase (H+-PPase; EC 3.6.1.1) is a unique enzyme playing a pivotal physiological role in pH homeostasis of organisms. This novel enzyme supplies energy at expense of hydrolyzing metabolic byproduct, pyrophosphate (PPi), for H+ translocation across membrane. The functional unit of a monomer suffices for enzymatic reaction of H+-PPase, while that for the translocation is homodimer. Its active site on each subunit consists of PPi binding motif, Acidic I and II motifs, and several essential residues. In this investigation, structural mapping of these vital regions was primarily determined utilizing single molecule fluorescence resonance energy transfer. Distances between two C termini and also two N termini on homodimeric subunits of H+-PPase are 49.3 ± 4.0 Å and 67.2 ± 5.7 Å, respectively. Furthermore, putative PPi binding motifs on individual subunits are found to be relatively far away from each other (70.8 ± 4.8 Å), while binding of potassium and substrate analogue led them to closer proximity (56.6 ± 4.1 Å). Moreover, substrate analogue but not potassium elicits significantly distance variations between two Acidic I motifs and two H622 residues on homodimeric subunits. Taken together, this study provides the first quantitative measurements of distances between various essential motifs, residues and putative active sites on homodimeric subunits of H+-PPase. A working model is accordingly proposed elucidating the distance variations of dimeric H+-PPase upon substrate binding.
Книги з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
service), ScienceDirect (Online, ed. Single molecule tools: Super-resolution, particle tracking, multiparameter and force based methods. San Diego, CA: Academic Press/Elsevier, 2010.
Знайти повний текст джерелаЧастини книг з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
Johnson-Buck, Alexander E., Mario R. Blanco, and Nils G. Walter. "Single-Molecule Fluorescence Resonance Energy Transfer." In Encyclopedia of Biophysics, 1–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-642-35943-9_492-1.
Повний текст джерелаJohnson-Buck, Alexander E., Mario R. Blanco, and Nils G. Walter. "Single-Molecule Fluorescence Resonance Energy Transfer." In Encyclopedia of Biophysics, 2329–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_492.
Повний текст джерелаLu, Ying, Jianbing Ma, and Ming Li. "Single-Molecule Biosensing by Fluorescence Resonance Energy Transfer." In Single-Molecule Tools for Bioanalysis, 79–120. Boca Raton: Jenny Stanford Publishing, 2022. http://dx.doi.org/10.1201/9781003189138-3.
Повний текст джерелаSpenkuch, Felix, Olwen Domingo, Gerald Hinze, Thomas Basché, and Mark Helm. "Studying RNA Using Single Molecule Fluorescence Resonance Energy Transfer." In Handbook of RNA Biochemistry, 499–526. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch24.
Повний текст джерелаFagerburg, Matt V., and Sanford H. Leuba. "Optimal Practices for Surface-Tethered Single Molecule Total Internal Reflection Fluorescence Resonance Energy Transfer Analysis." In DNA Nanotechnology, 273–89. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-142-0_19.
Повний текст джерелаMacDougall, Daniel D., and Ruben L. Gonzalez. "Exploring the structural dynamics of the translational machinery using single-molecule fluorescence resonance energy transfer." In Ribosomes, 273–93. Vienna: Springer Vienna, 2011. http://dx.doi.org/10.1007/978-3-7091-0215-2_22.
Повний текст джерелаChoi, Ucheor B., Keith R. Weninger, and Mark E. Bowen. "Immobilization of Proteins for Single-Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics." In Intrinsically Disordered Protein Analysis, 3–20. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3704-8_1.
Повний текст джерелаAndreou, Alexandra Z., and Dagmar Klostermeier. "Conformational Changes of DEAD-Box Helicases Monitored by Single Molecule Fluorescence Resonance Energy Transfer." In Methods in Enzymology, 75–109. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-396546-2.00004-8.
Повний текст джерелаHan, Jun, Erwen Mei, Mei-Ping Kung, Hank F. Kung, Jian-Min Yuan, and Hai-Lung Dai. "Single-Molecule Fluorescence Resonance Energy Transfer Studies of β-Amyloid Clusters in Physiological Solutions." In Biophysics and Biochemistry of Protein Aggregation, 297–311. World Scientific, 2017. http://dx.doi.org/10.1142/9789813202382_0008.
Повний текст джерелаGreenfeld, Max, and Daniel Herschlag. "Measuring the Energetic Coupling of Tertiary Contacts in RNA Folding using Single Molecule Fluorescence Resonance Energy Transfer." In Methods in Enzymology, 205–20. Elsevier, 2010. http://dx.doi.org/10.1016/s0076-6879(10)72009-7.
Повний текст джерелаТези доповідей конференцій з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
Ernst, S., B. Verhalen, N. Zarrabi, S. Wilkens, and M. Börsch. "Drug transport mechanism of P-glycoprotein monitored by single molecule fluorescence resonance energy transfer." In SPIE BiOS, edited by Ammasi Periasamy, Karsten König, and Peter T. C. So. SPIE, 2011. http://dx.doi.org/10.1117/12.872989.
Повний текст джерелаCotlet, Mircea, Tom Vosch, Sadahiro Masuo, Marcus Sauer, Klaus Muellen, Johan Hofkens, and Frans De Schryver. "Single-molecule spectroscopy to probe competitive fluorescence resonance energy transfer pathways in bichromophoric synthetic systems." In Biomedical Optics 2004, edited by Dan V. Nicolau, Joerg Enderlein, Robert C. Leif, and Daniel L. Farkas. SPIE, 2004. http://dx.doi.org/10.1117/12.531322.
Повний текст джерелаFore, Samantha, Thomas Huser, Yin Yuen, and Lambertus Hesselink. "Single Molecule Pulsed Interleaved Excitation Fluorescence Resonance Energy Transfer (PIE-FRET) inside Nanometer-scale Apertures at Biologically Relevant Concentration." In CLEO 2007. IEEE, 2007. http://dx.doi.org/10.1109/cleo.2007.4453191.
Повний текст джерелаYeh, Hsin-Chih, Christopher M. Puleo, Yi-Ping Ho, and Tza-Huei Wang. "Towards Single-Molecule Diagnostics Using Microfluidic Manipulation and Quantum Dot Nanosensors." In ASME 2007 5th International Conference on Nanochannels, Microchannels, and Minichannels. ASMEDC, 2007. http://dx.doi.org/10.1115/icnmm2007-30213.
Повний текст джерелаTsourkas, Andrew, Jason Xu, and Gang Bao. "Hybridization Dynamics and Kinetics of Fret-Enhanced Molecular Beacons." In ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/bed-23163.
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