Статті в журналах з теми "Rapid resonance assignment of proteins"
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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 джерелаFox, Daniel A., та Linda Columbus. "Solution NMR resonance assignment strategies for β-barrel membrane proteins". Protein Science 22, № 8 (27 червня 2013): 1133–40. http://dx.doi.org/10.1002/pro.2291.
Повний текст джерелаTrbovic, Nikola, Christian Klammt, Alexander Koglin, Frank Löhr, Frank Bernhard, and Volker Dötsch. "Efficient Strategy for the Rapid Backbone Assignment of Membrane Proteins." Journal of the American Chemical Society 127, no. 39 (October 2005): 13504–5. http://dx.doi.org/10.1021/ja0540270.
Повний текст джерелаALIPANAHI, BABAK, XIN GAO, EMRE KARAKOC, SHUAI CHENG Li, FRANK BALBACH, GUANGYU FENG, LOGAN DONALDSON, and MING LI. "ERROR TOLERANT NMR BACKBONE RESONANCE ASSIGNMENT AND AUTOMATED STRUCTURE GENERATION." Journal of Bioinformatics and Computational Biology 09, no. 01 (February 2011): 15–41. http://dx.doi.org/10.1142/s0219720011005276.
Повний текст джерелаPannetier, Nicolas, Klaartje Houben, Laurence Blanchard, and Dominique Marion. "Optimized 3D-NMR sampling for resonance assignment of partially unfolded proteins." Journal of Magnetic Resonance 186, no. 1 (May 2007): 142–49. http://dx.doi.org/10.1016/j.jmr.2007.01.013.
Повний текст джерелаLeopold, M. F., Jeffrey L. Urbauer, and A. Joshua Wand. "Resonance assignment strategies for the analysis of nmr spectra of proteins." Molecular Biotechnology 2, no. 1 (August 1994): 61–93. http://dx.doi.org/10.1007/bf02789290.
Повний текст джерелаPiai, Alessandro, Leonardo Gonnelli, Isabella C. Felli, Roberta Pierattelli, Krzysztof Kazimierczuk, Katarzyna Grudziąż, Wiktor Koźmiński, and Anna Zawadzka-Kazimierczuk. "Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins." Journal of Biomolecular NMR 64, no. 3 (February 18, 2016): 239–53. http://dx.doi.org/10.1007/s10858-016-0024-2.
Повний текст джерелаLi, Kuo-Bin, and B. C. Sanctuary. "Automated Resonance Assignment of Proteins Using Heteronuclear 3D NMR. 2. Side Chain and Sequence-Specific Assignment." Journal of Chemical Information and Computer Sciences 37, no. 3 (May 1997): 467–77. http://dx.doi.org/10.1021/ci960372k.
Повний текст джерелаKnox, Robert W., George J. Lu, Stanley J. Opella, and Alexander A. Nevzorov. "A Resonance Assignment Method for Oriented-Sample Solid-State NMR of Proteins." Journal of the American Chemical Society 132, no. 24 (June 23, 2010): 8255–57. http://dx.doi.org/10.1021/ja102932n.
Повний текст джерелаGossert, Alvar D., Sebastian Hiller, and César Fernández. "Automated NMR Resonance Assignment of Large Proteins for Protein−Ligand Interaction Studies." Journal of the American Chemical Society 133, no. 2 (January 19, 2011): 210–13. http://dx.doi.org/10.1021/ja108383x.
Повний текст джерелаWei, Qingtao, Jiajing Chen, Juan Mi, Jiahai Zhang, Ke Ruan та Jihui Wu. "NMR Backbone Assignment of Large Proteins by Using13Cα-Only Triple-Resonance Experiments". Chemistry - A European Journal 22, № 28 (8 червня 2016): 9556–64. http://dx.doi.org/10.1002/chem.201601871.
Повний текст джерелаKarjalainen, Mikael, Helena Tossavainen, Maarit Hellman та Perttu Permi. "HACANCOi: a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins". Journal of Biomolecular NMR 74, № 12 (28 жовтня 2020): 741–52. http://dx.doi.org/10.1007/s10858-020-00347-5.
Повний текст джерелаBarbet-Massin, Emeline, Andrew J. Pell, Joren S. Retel, Loren B. Andreas, Kristaps Jaudzems, W. Trent Franks, Andrew J. Nieuwkoop, et al. "Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning." Journal of the American Chemical Society 136, no. 35 (August 18, 2014): 12489–97. http://dx.doi.org/10.1021/ja507382j.
Повний текст джерелаMorris, Howard R., and Piero Pucci. "A new method for rapid assignment of S-S bridges in proteins." Biochemical and Biophysical Research Communications 126, no. 3 (February 1985): 1122–28. http://dx.doi.org/10.1016/0006-291x(85)90302-x.
Повний текст джерелаLin, Guohui, Dong Xu, Zhi-Zhong Chen, Tao Jiang, Jianjun Wen, and Ying Xu. "Computational Assignment of Protein Backbone NMR Peaks by Efficient Bounding and Filtering." Journal of Bioinformatics and Computational Biology 01, no. 02 (July 2003): 387–409. http://dx.doi.org/10.1142/s0219720003000083.
Повний текст джерелаHiller, Sebastian, Christian Wasmer, Gerhard Wider, and Kurt Wüthrich. "Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy." Journal of the American Chemical Society 129, no. 35 (September 2007): 10823–28. http://dx.doi.org/10.1021/ja072564+.
Повний текст джерелаCutting, Brian, André Strauss, Gabriele Fendrich, Paul W. Manley, and Wolfgang Jahnke. "NMR resonance assignment of selectively labeled proteins by the use of paramagnetic ligands." Journal of Biomolecular NMR 30, no. 2 (October 2004): 205–10. http://dx.doi.org/10.1023/b:jnmr.0000048947.28598.ea.
Повний текст джерелаSchubert, Mario, Michael Kolbe, Brigitte Kessler, Dieter Oesterhelt, and Peter Schmieder. "Heteronuclear Multidimensional NMR Spectroscopy of Solubilized Membrane Proteins: Resonance Assignment of Native Bacteriorhodopsin." ChemBioChem 3, no. 10 (October 4, 2002): 1019–23. http://dx.doi.org/10.1002/1439-7633(20021004)3:10<1019::aid-cbic1019>3.0.co;2-c.
Повний текст джерелаSolyom, Zsofia, Melanie Schwarten, Leonhard Geist, Robert Konrat, Dieter Willbold, and Bernhard Brutscher. "BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins." Journal of Biomolecular NMR 55, no. 4 (February 24, 2013): 311–21. http://dx.doi.org/10.1007/s10858-013-9715-0.
Повний текст джерелаSchmidt, Elena, and Peter Güntert. "Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins." Journal of Biomolecular NMR 57, no. 2 (September 15, 2013): 193–204. http://dx.doi.org/10.1007/s10858-013-9779-x.
Повний текст джерелаShcherbakov, Alexander A., Matthias Roos, Byungsu Kwon, and Mei Hong. "Two-dimensional 19F–13C correlation NMR for 19F resonance assignment of fluorinated proteins." Journal of Biomolecular NMR 74, no. 2-3 (February 22, 2020): 193–204. http://dx.doi.org/10.1007/s10858-020-00306-0.
Повний текст джерелаKumar, Dinesh, Subhradip Paul, and Ramakrishna V. Hosur. "BEST-HNN and 2D-(HN)NH experiments for rapid backbone assignment in proteins." Journal of Magnetic Resonance 204, no. 1 (May 2010): 111–17. http://dx.doi.org/10.1016/j.jmr.2010.02.013.
Повний текст джерелаAverseng, Olivier, Agnès Hagège, Frédéric Taran, and Claude Vidaud. "Surface Plasmon Resonance for Rapid Screening of Uranyl Affine Proteins." Analytical Chemistry 82, no. 23 (December 2010): 9797–802. http://dx.doi.org/10.1021/ac102578y.
Повний текст джерелаLI, K. B., and B. C. SANCTUARY. "ChemInform Abstract: Automated Resonance Assignment of Proteins Using Heteronuclear 3D NMR. Part 2. Side Chain and Sequence-Specific Assignment." ChemInform 28, no. 37 (August 3, 2010): no. http://dx.doi.org/10.1002/chin.199737284.
Повний текст джерелаRomero, Javier A., Paulina Putko, Mateusz Urbańczyk, Krzysztof Kazimierczuk, and Anna Zawadzka-Kazimierczuk. "Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins." PLOS Computational Biology 18, no. 10 (October 6, 2022): e1010258. http://dx.doi.org/10.1371/journal.pcbi.1010258.
Повний текст джерелаSong, Sunho, Sanford A. Asher, Samuel Krimm, and Jagdeesh Bandekar. "Assignment of a new conformation-sensitive UV resonance Raman band in peptides and proteins." Journal of the American Chemical Society 110, no. 25 (December 1988): 8547–48. http://dx.doi.org/10.1021/ja00233a042.
Повний текст джерелаSalzmann, M., K. Pervushin, G. Wider, H. Senn, and K. Wuthrich. "TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins." Proceedings of the National Academy of Sciences 95, no. 23 (November 10, 1998): 13585–90. http://dx.doi.org/10.1073/pnas.95.23.13585.
Повний текст джерелаFeuerstein, Sophie, Michael J. Plevin, Dieter Willbold, and Bernhard Brutscher. "iHADAMAC: A complementary tool for sequential resonance assignment of globular and highly disordered proteins." Journal of Magnetic Resonance 214 (January 2012): 329–34. http://dx.doi.org/10.1016/j.jmr.2011.10.019.
Повний текст джерелаWilliams, Robert V., Monique J. Rogals, Alexander Eletsky, Chin Huang, Laura C. Morris, Kelley W. Moremen, and James H. Prestegard. "AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins." Journal of Magnetic Resonance 345 (December 2022): 107336. http://dx.doi.org/10.1016/j.jmr.2022.107336.
Повний текст джерелаLöhr, Frank, and Heinz Rüterjans. "A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins." Journal of Biomolecular NMR 6, no. 2 (September 1995): 189–97. http://dx.doi.org/10.1007/bf00211783.
Повний текст джерелаMedvedeva, Svetlana, Jean-Pierre Simorre, Bernhard Brutscher, Françoise Guerlesquin, and Dominique Marion. "Extensive1H NMR resonance assignment of proteins using natural abundance gradient-enhanced13C−1H correlation spectroscopy." FEBS Letters 333, no. 3 (November 1, 1993): 251–56. http://dx.doi.org/10.1016/0014-5793(93)80664-g.
Повний текст джерелаLöhr, Frank, and Heinz Rüterjans. "Novel Pulse Sequences for the Resonance Assignment of Aromatic Side Chains in13C-Labeled Proteins." Journal of Magnetic Resonance, Series B 112, no. 3 (September 1996): 259–68. http://dx.doi.org/10.1006/jmrb.1996.0140.
Повний текст джерелаPlevin, Michael J., Olivier Hamelin, Jérôme Boisbouvier, and Pierre Gans. "A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins." Journal of Biomolecular NMR 49, no. 2 (February 2011): 61–67. http://dx.doi.org/10.1007/s10858-010-9463-3.
Повний текст джерелаIuga, Adriana, Michael Spoerner, Christian Ader, Eike Brunner, and Hans Robert Kalbitzer. "Rapid assignment of solution 31P NMR spectra of large proteins by solid-state spectroscopy." Biochemical and Biophysical Research Communications 346, no. 1 (July 2006): 301–5. http://dx.doi.org/10.1016/j.bbrc.2006.05.116.
Повний текст джерелаBoyko, Kristina V., Erin A. Rosenkranz, Derrick M. Smith, Heather L. Miears, Melissa Oueld es cheikh, Micah Z. Lund, Jeffery C. Young, et al. "Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins." PLOS ONE 16, no. 10 (October 28, 2021): e0258531. http://dx.doi.org/10.1371/journal.pone.0258531.
Повний текст джерелаJang, Richard, Xin Gao, and Ming Li. "Towards Fully Automated Structure-Based NMR Resonance Assignment of15N-Labeled Proteins From Automatically Picked Peaks." Journal of Computational Biology 18, no. 3 (March 2011): 347–63. http://dx.doi.org/10.1089/cmb.2010.0251.
Повний текст джерелаZawadzka-Kazimierczuk, Anna, Krzysztof Kazimierczuk, and Wiktor Koźmiński. "A set of 4D NMR experiments of enhanced resolution for easy resonance assignment in proteins." Journal of Magnetic Resonance 202, no. 1 (January 2010): 109–16. http://dx.doi.org/10.1016/j.jmr.2009.10.006.
Повний текст джерелаWen, Jie, Jihui Wu, and Pei Zhou. "Sparsely sampled high-resolution 4-D experiments for efficient backbone resonance assignment of disordered proteins." Journal of Magnetic Resonance 209, no. 1 (March 2011): 94–100. http://dx.doi.org/10.1016/j.jmr.2010.12.012.
Повний текст джерелаBoucher, Wayne, Ernest D. Laue, Sharon Campbell-Burk, and Peter J. Domaille. "Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins." Journal of the American Chemical Society 114, no. 6 (March 1992): 2262–64. http://dx.doi.org/10.1021/ja00032a053.
Повний текст джерелаStratmann, Dirk, Carine van Heijenoort, and Eric Guittet. "NOEnet–Use of NOE networks for NMR resonance assignment of proteins with known 3D structure." Bioinformatics 25, no. 4 (December 12, 2008): 474–81. http://dx.doi.org/10.1093/bioinformatics/btn638.
Повний текст джерелаMcIntosh, Lawrence P., and Frederick W. Dahlquist. "Biosynthetic Incorporation of15N and13C for Assignment and Interpretation of Nuclear Magnetic Resonance Spectra of Proteins." Quarterly Reviews of Biophysics 23, no. 1 (February 1990): 1–38. http://dx.doi.org/10.1017/s0033583500005400.
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