Literatura académica sobre el tema "Rapid resonance assignment of proteins"
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Artículos de revistas sobre el tema "Rapid resonance assignment of proteins"
Fredriksson, Jonas, Wolfgang Bermel y Martin Billeter. "Complete protein assignment from sets of spectra recorded overnight". Journal of Biomolecular NMR 73, n.º 1-2 (15 de febrero de 2019): 59–70. http://dx.doi.org/10.1007/s10858-019-00226-8.
Texto completoRout, Ashok K., Ravi P. Barnwal, Geetika Agarwal y Kandala V. R. Chary. "Root-mean-square-deviation-based rapid backbone resonance assignments in proteins". Magnetic Resonance in Chemistry 48, n.º 10 (27 de agosto de 2010): 793–97. http://dx.doi.org/10.1002/mrc.2664.
Texto completoSukumaran, Sujeesh, Shahid A. Malik, Shankararama Sharma R., Kousik Chandra y Hanudatta S. Atreya. "Rapid NMR assignments of intrinsically disordered proteins using two-dimensional13C-detection based experiments". Chemical Communications 55, n.º 54 (2019): 7820–23. http://dx.doi.org/10.1039/c9cc03530c.
Texto completoChatterjee, Amarnath, Neel S. Bhavesh, Sanjay C. Panchal y 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, n.º 1 (abril de 2002): 427–32. http://dx.doi.org/10.1016/s0006-291x(02)00240-1.
Texto completoKostic, Milka, Susan Sondej Pochapsky y 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, n.º 31 (agosto de 2002): 9054–55. http://dx.doi.org/10.1021/ja0268480.
Texto completoVendrell, J., F. X. Avilés, M. Vilanova, C. H. Turner y C. Crane-Robinson. "1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A". Biochemical Journal 267, n.º 1 (1 de abril de 1990): 213–20. http://dx.doi.org/10.1042/bj2670213.
Texto completoKumar, Dinesh y 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, n.º 9 (5 de agosto de 2011): 575–83. http://dx.doi.org/10.1002/mrc.2787.
Texto completoFiorito, Francesco, Sebastian Hiller, Gerhard Wider y Kurt Wüthrich. "Automated Resonance Assignment of Proteins: 6 DAPSY-NMR". Journal of Biomolecular NMR 35, n.º 1 (mayo de 2006): 27–37. http://dx.doi.org/10.1007/s10858-006-0030-x.
Texto completoHigman, Victoria A. "Solid-state MAS NMR resonance assignment methods for proteins". Progress in Nuclear Magnetic Resonance Spectroscopy 106-107 (junio de 2018): 37–65. http://dx.doi.org/10.1016/j.pnmrs.2018.04.002.
Texto completoCrippen, Gordon M., Aikaterini Rousaki, Matthew Revington, Yongbo Zhang y Erik R. P. Zuiderweg. "SAGA: rapid automatic mainchain NMR assignment for large proteins". Journal of Biomolecular NMR 46, n.º 4 (16 de marzo de 2010): 281–98. http://dx.doi.org/10.1007/s10858-010-9403-2.
Texto completoTesis sobre el tema "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.
Texto completoLi, 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.
Texto completoHelgstrand, 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.
Texto completoHabenstein, Birgit. "Structural insights into fibrillar proteins from solid-state NMR spectroscopy". Thesis, Lyon 1, 2011. http://www.theses.fr/2011LYO10212.
Texto completoSolid-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 y 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.
Texto completoSujeesh, K. S. "New NMR Methods with high resolution and sensitivity for rapid data analysis". Thesis, 2019. https://etd.iisc.ac.in/handle/2005/5041.
Texto completoDubey, Abhinav. "Development Of NMR Methods For Metabolomics And Protein Resonance Assignments". Thesis, 2016. https://etd.iisc.ac.in/handle/2005/2633.
Texto completoDubey, Abhinav. "Development Of NMR Methods For Metabolomics And Protein Resonance Assignments". Thesis, 2016. http://etd.iisc.ernet.in/handle/2005/2633.
Texto completo"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.
Texto completoFranks, 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.
Texto completoSource: 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.
Capítulos de libros sobre el tema "Rapid resonance assignment of proteins"
Robertson, Andrew D. y John L. Markley. "Methods of Proton Resonance Assignment for Proteins". En Biological Magnetic Resonance, 155–76. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-6549-9_4.
Texto completoRedfield, Christina y James P. Robertson. "Assignment of the NMR Spectra of Homologous Proteins". En 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.
Texto completoKleywegt, Gerard J., Rolf Boelens y Robert Kaptein. "STELLA and CLAIRE: A Seraglio of Programs for Human-Aided Assignment of 2D 1H NMR Spectra of Proteins". En 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.
Texto completoHiller, Sebastian, Christian Wasmer, Gerhard Wider y Kurt Wüthrich. "Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy". En NMR with Biological Macromolecules in Solution, 72–77. WORLD SCIENTIFIC, 2021. http://dx.doi.org/10.1142/9789811235795_0008.
Texto completoDijkgraaf, Ingrid, Stijn M. Agten, Matthias Bauwens y Tilman M. Hackeng. "Strategies for Site-Specific Radiolabeling of Peptides and Proteins". En Radiopharmaceuticals [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.99422.
Texto completoKaplan, O. y J. S. Cohen. "Nuclear Magnetic Resonance Spectroscopy Studies of Cancer Cell Metabolism". En Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0030.
Texto completoMcKeon, Andrew y Nicholas L. Zalewski. "Rapid-Onset Hemibody Sensory Loss, Incoordination, and Muscle Jerking". En Mayo Clinic Cases in Neuroimmunology, editado por Andrew McKeon, B. Mark Keegan y W. Oliver Tobin, 184–86. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780197583425.003.0059.
Texto completoMatthews, K. S. y R. Matthews. "Selective Chemical Deuteration of Aromatic Amino Acids: A Retrospective". En Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0021.
Texto completoGraves, Steven W. y John P. Nolan. "Molecular Assemblies, Probes, and Proteomics in Flow Cytometry". En Flow Cytometry for Biotechnology. Oxford University Press, 2005. http://dx.doi.org/10.1093/oso/9780195183146.003.0013.
Texto completoActas de conferencias sobre el tema "Rapid resonance assignment of proteins"
Champion, P. M., J. T. Sage y P. Li. "Resonance Raman Studies of Electronic and Vibrational Relaxation Dynamics in Heme Proteins". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.tuc6.
Texto completoFuris, B. C., M. J. Jorgensem, M. J. Rabiet, A. B. Contor, C. L. Brown, C. B. Shoemaker y B. Furie. "RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.
Texto completoMcCarthy, Michael C. y R. W. Field. "Application of a sideband oodr Zeeman spectroscopy to diatomic molecules". En OSA Annual Meeting. Washington, D.C.: Optica Publishing Group, 1990. http://dx.doi.org/10.1364/oam.1990.wn2.
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