Добірка наукової літератури з теми "Rapid resonance assignment of proteins"
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Статті в журналах з теми "Rapid resonance assignment of proteins"
Fredriksson, Jonas, Wolfgang Bermel, and Martin Billeter. "Complete protein assignment from sets of spectra recorded overnight." Journal of Biomolecular NMR 73, no. 1-2 (February 15, 2019): 59–70. http://dx.doi.org/10.1007/s10858-019-00226-8.
Повний текст джерелаRout, Ashok K., Ravi P. Barnwal, Geetika Agarwal, and Kandala V. R. Chary. "Root-mean-square-deviation-based rapid backbone resonance assignments in proteins." Magnetic Resonance in Chemistry 48, no. 10 (August 27, 2010): 793–97. http://dx.doi.org/10.1002/mrc.2664.
Повний текст джерелаSukumaran, Sujeesh, Shahid A. Malik, Shankararama Sharma R., Kousik Chandra, and Hanudatta S. Atreya. "Rapid NMR assignments of intrinsically disordered proteins using two-dimensional13C-detection based experiments." Chemical Communications 55, no. 54 (2019): 7820–23. http://dx.doi.org/10.1039/c9cc03530c.
Повний текст джерелаChatterjee, Amarnath, Neel S. Bhavesh, Sanjay C. Panchal, and Ramakrishna V. Hosur. "A novel protocol based on HN(C)N for rapid resonance assignment in (15N, 13C) labeled proteins: implications to structural genomics." Biochemical and Biophysical Research Communications 293, no. 1 (April 2002): 427–32. http://dx.doi.org/10.1016/s0006-291x(02)00240-1.
Повний текст джерелаKostic, Milka, Susan Sondej Pochapsky, and Thomas C. Pochapsky. "Rapid Recycle13C‘,15N and13C,13C‘ Heteronuclear and Homonuclear Multiple Quantum Coherence Detection for Resonance Assignments in Paramagnetic Proteins: Example of Ni2+-Containing Acireductone Dioxygenase." Journal of the American Chemical Society 124, no. 31 (August 2002): 9054–55. http://dx.doi.org/10.1021/ja0268480.
Повний текст джерелаVendrell, J., F. X. Avilés, M. Vilanova, C. H. Turner, and C. Crane-Robinson. "1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A." Biochemical Journal 267, no. 1 (April 1, 1990): 213–20. http://dx.doi.org/10.1042/bj2670213.
Повний текст джерелаKumar, Dinesh, and Ramakrishna V. Hosur. "hNCOcanH pulse sequence and a robust protocol for rapid and unambiguous assignment of backbone (1 HN , 15 N and 13 C′) resonances in 15 N/13 C-labeled proteins." Magnetic Resonance in Chemistry 49, no. 9 (August 5, 2011): 575–83. http://dx.doi.org/10.1002/mrc.2787.
Повний текст джерелаFiorito, Francesco, Sebastian Hiller, Gerhard Wider, and Kurt Wüthrich. "Automated Resonance Assignment of Proteins: 6 DAPSY-NMR." Journal of Biomolecular NMR 35, no. 1 (May 2006): 27–37. http://dx.doi.org/10.1007/s10858-006-0030-x.
Повний текст джерелаHigman, Victoria A. "Solid-state MAS NMR resonance assignment methods for proteins." Progress in Nuclear Magnetic Resonance Spectroscopy 106-107 (June 2018): 37–65. http://dx.doi.org/10.1016/j.pnmrs.2018.04.002.
Повний текст джерелаCrippen, Gordon M., Aikaterini Rousaki, Matthew Revington, Yongbo Zhang, and Erik R. P. Zuiderweg. "SAGA: rapid automatic mainchain NMR assignment for large proteins." Journal of Biomolecular NMR 46, no. 4 (March 16, 2010): 281–98. http://dx.doi.org/10.1007/s10858-010-9403-2.
Повний текст джерелаДисертації з теми "Rapid resonance assignment of proteins"
Jung, Young-Sang. "Rapid determination of protein structures in solution using NMR dipolar couplings." Doctoral thesis, [S.l.] : [s.n.], 2005. http://webdoc.sub.gwdg.de/diss/2005/jung/jung.pdf.
Повний текст джерелаLi, Kuo-Bin. "Development of computer-assisted methods for the resonance assignment of heteronuclear 3D NMR spectra of proteins." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40381.
Повний текст джерелаHelgstrand, Magnus. "Structure determination of ribosomal proteins and development of new methods in biomolecular NMR." Doctoral thesis, Stockholm : Tekniska högsk, 2001. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3149.
Повний текст джерелаHabenstein, Birgit. "Structural insights into fibrillar proteins from solid-state NMR spectroscopy." Thesis, Lyon 1, 2011. http://www.theses.fr/2011LYO10212.
Повний текст джерелаSolid-state NMR is the method of choice for studies on insoluble proteins and other high molecular weight protein complexes. The inherent insolubility of fibrillar proteins, as well as their complex architecture, makes the application of x-ray crystallography and solution state NMR difficult. Solid-state NMR is not limited by the molecular weight or by the absence of long-range structural order, and is thus a powerful tool for the 3D structural investigation of fibrillar proteins. The assignment of the NMR resonances is a prerequisite to obtain structural information at atomic level. The first part of this thesis describes the development of solid-state NMR methods to assign the resonances in large proteins. We apply these methods to assign the 33 kDa C-terminal domain of the Ure2p prion which is up to now the largest protein assigned by solid-state NMR. Our results provide the basis to study high molecular weight proteins at atomic level. This is demonstrated in the second part with the first high-resolution solid-state NMR study of Ure2 and Sup35 prion fibrils. We describe the conformation of the functional domains and prion domains in the full-length fibrils and in isolation. The third fibrillar protein addressed in this work is the Parkinson’s disease related α-synuclein whereof we demonstrate the NMR resonance assignment and the secondary structure determination of a new polymorph. Thus, the studies described here provide new insights in the structural diversity of fibril architectures, and plead to view fibrils as individuals from a structural point of view, rather than a homogenous protein family
Yao, Xuejun [Verfasser], Markus [Akademischer Betreuer] Zweckstetter, and Kai [Akademischer Betreuer] Tittmann. "Solution NMR-based characterization of the structure of the outer mitochondrial membrane protein Tom40 and a novel method for NMR resonance assignment of large intrinsically disordered proteins / Xuejun Yao. Gutachter: Markus Zweckstetter ; Kai Tittmann. Betreuer: Markus Zweckstetter." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2014. http://d-nb.info/1050873122/34.
Повний текст джерелаSujeesh, K. S. "New NMR Methods with high resolution and sensitivity for rapid data analysis." Thesis, 2019. https://etd.iisc.ac.in/handle/2005/5041.
Повний текст джерелаDubey, Abhinav. "Development Of NMR Methods For Metabolomics And Protein Resonance Assignments." Thesis, 2016. https://etd.iisc.ac.in/handle/2005/2633.
Повний текст джерелаDubey, Abhinav. "Development Of NMR Methods For Metabolomics And Protein Resonance Assignments." Thesis, 2016. http://etd.iisc.ernet.in/handle/2005/2633.
Повний текст джерела"Biomolecular solid-state nuclear magnetic resonance methods for spectral assignment and high-resolution structure determination of proteins." UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN, 2008. http://pqdtopen.proquest.com/#viewpdf?dispub=3301264.
Повний текст джерелаFranks, William Trent. "Biomolecular solid-state nuclear magnetic resonance methods for spectral assignment and high-resolution structure determination of proteins /." 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3301264.
Повний текст джерелаSource: Dissertation Abstracts International, Volume: 69-02, Section: B, page: 1027. Adviser: Chad M. Rienstra. Includes supplementary digital materials. Includes bibliographical references. Available on microfilm from Pro Quest Information and Learning.
Частини книг з теми "Rapid resonance assignment of proteins"
Robertson, Andrew D., and John L. Markley. "Methods of Proton Resonance Assignment for Proteins." In Biological Magnetic Resonance, 155–76. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-6549-9_4.
Повний текст джерелаRedfield, Christina, and James P. Robertson. "Assignment of the NMR Spectra of Homologous Proteins." In Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy, 303–16. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9794-7_23.
Повний текст джерелаKleywegt, Gerard J., Rolf Boelens, and Robert Kaptein. "STELLA and CLAIRE: A Seraglio of Programs for Human-Aided Assignment of 2D 1H NMR Spectra of Proteins." In Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy, 427–37. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9794-7_34.
Повний текст джерелаHiller, Sebastian, Christian Wasmer, Gerhard Wider, and Kurt Wüthrich. "Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy." In NMR with Biological Macromolecules in Solution, 72–77. WORLD SCIENTIFIC, 2021. http://dx.doi.org/10.1142/9789811235795_0008.
Повний текст джерелаDijkgraaf, Ingrid, Stijn M. Agten, Matthias Bauwens, and Tilman M. Hackeng. "Strategies for Site-Specific Radiolabeling of Peptides and Proteins." In Radiopharmaceuticals [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.99422.
Повний текст джерелаKaplan, O., and J. S. Cohen. "Nuclear Magnetic Resonance Spectroscopy Studies of Cancer Cell Metabolism." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0030.
Повний текст джерелаMcKeon, Andrew, and Nicholas L. Zalewski. "Rapid-Onset Hemibody Sensory Loss, Incoordination, and Muscle Jerking." In Mayo Clinic Cases in Neuroimmunology, edited by Andrew McKeon, B. Mark Keegan, and W. Oliver Tobin, 184–86. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780197583425.003.0059.
Повний текст джерелаMatthews, K. S., and R. Matthews. "Selective Chemical Deuteration of Aromatic Amino Acids: A Retrospective." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0021.
Повний текст джерелаGraves, Steven W., and John P. Nolan. "Molecular Assemblies, Probes, and Proteomics in Flow Cytometry." In Flow Cytometry for Biotechnology. Oxford University Press, 2005. http://dx.doi.org/10.1093/oso/9780195183146.003.0013.
Повний текст джерелаТези доповідей конференцій з теми "Rapid resonance assignment of proteins"
Champion, P. M., J. T. Sage, and P. Li. "Resonance Raman Studies of Electronic and Vibrational Relaxation Dynamics in Heme Proteins." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.tuc6.
Повний текст джерелаFuris, B. C., M. J. Jorgensem, M. J. Rabiet, A. B. Contor, C. L. Brown, C. B. Shoemaker, and B. Furie. "RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.
Повний текст джерелаMcCarthy, Michael C., and R. W. Field. "Application of a sideband oodr Zeeman spectroscopy to diatomic molecules." In OSA Annual Meeting. Washington, D.C.: Optica Publishing Group, 1990. http://dx.doi.org/10.1364/oam.1990.wn2.
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