Log in

Relevant bibliographies by topics / Rapid resonance assignment of proteins / Journal articles

To see the other types of publications on this topic, follow the link: Rapid resonance assignment of proteins.

Journal articles on the topic 'Rapid resonance assignment of proteins'

Author: Grafiati

Published: 6 September 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Rapid resonance assignment of proteins.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Fredriksson, Jonas, Wolfgang Bermel, and Martin Billeter. "Complete protein assignment from sets of spectra recorded overnight." Journal of Biomolecular NMR 73, no. 1-2 (2019): 59–70. http://dx.doi.org/10.1007/s10858-019-00226-8.

Full text

Abstract:

Abstract A flexible and scalable approach for protein NMR is introduced that builds on rapid data collection via projection spectroscopy and analysis of the spectral input data via joint decomposition. Input data may originate from various types of spectra, depending on the ultimate goal: these may result from experiments based on triple-resonance pulse sequences, or on TOCSY or NOESY sequences, or mixtures thereof. Flexible refers to the free choice of spectra for the joint decompositions depending on the purpose: assignments, structure, dynamics, interactions. Scalable means that the approac

APA, Harvard, Vancouver, ISO, and other styles

2

Rout, 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 (2010): 793–97. http://dx.doi.org/10.1002/mrc.2664.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Sukumaran, 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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Chatterjee, 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 (2002): 427–32. http://dx.doi.org/10.1016/s0006-291x(02)00240-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Kostic, 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 (2002): 9054–55. http://dx.doi.org/10.1021/ja0268480.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Vendrell, 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 (1990): 213–20. http://dx.doi.org/10.1042/bj2670213.

Full text

Abstract:

The isolated activation segment (asA) from pig pancreatic procarboxypeptidase A was studied by 1H-n.m.r. spectroscopy over a wide range of solution conditions. Isolated asA shows many characteristics of compactly folded globular proteins, such as the observation of perturbed positions for resonances from methyl groups, alpha-carbon atoms, histidine residues and the tyrosine residue. The single tyrosine residue (Tyr-70) exhibits a very high pKa, and both histidine and tyrosine residues show slow chemical modification (deuteration and iodination). In contrast, asA shows rapid NH exchange. Analys

APA, Harvard, Vancouver, ISO, and other styles

7

Kumar, 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 (2011): 575–83. http://dx.doi.org/10.1002/mrc.2787.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Fiorito, Francesco, Sebastian Hiller, Gerhard Wider, and Kurt Wüthrich. "Automated Resonance Assignment of Proteins: 6 DAPSY-NMR." Journal of Biomolecular NMR 35, no. 1 (2006): 27–37. http://dx.doi.org/10.1007/s10858-006-0030-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Higman, 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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Crippen, 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 (2010): 281–98. http://dx.doi.org/10.1007/s10858-010-9403-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Fox, Daniel A., та Linda Columbus. "Solution NMR resonance assignment strategies for β-barrel membrane proteins". Protein Science 22, № 8 (2013): 1133–40. http://dx.doi.org/10.1002/pro.2291.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Trbovic, 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 (2005): 13504–5. http://dx.doi.org/10.1021/ja0540270.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

ALIPANAHI, BABAK, XIN GAO, EMRE KARAKOC, et al. "ERROR TOLERANT NMR BACKBONE RESONANCE ASSIGNMENT AND AUTOMATED STRUCTURE GENERATION." Journal of Bioinformatics and Computational Biology 09, no. 01 (2011): 15–41. http://dx.doi.org/10.1142/s0219720011005276.

Full text

Abstract:

Error tolerant backbone resonance assignment is the cornerstone of the NMR structure determination process. Although a variety of assignment approaches have been developed, none works sufficiently well on noisy fully automatically picked peaks to enable the subsequent automatic structure determination steps. We have designed an integer linear programming (ILP) based assignment system (IPASS) that has enabled fully automatic protein structure determination for four test proteins. IPASS employs probabilistic spin system typing based on chemical shifts and secondary structure predictions. Further

APA, Harvard, Vancouver, ISO, and other styles

14

Pannetier, 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 (2007): 142–49. http://dx.doi.org/10.1016/j.jmr.2007.01.013.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Leopold, 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 (1994): 61–93. http://dx.doi.org/10.1007/bf02789290.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Piai, Alessandro, Leonardo Gonnelli, Isabella C. Felli, et al. "Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins." Journal of Biomolecular NMR 64, no. 3 (2016): 239–53. http://dx.doi.org/10.1007/s10858-016-0024-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Li, 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 (1997): 467–77. http://dx.doi.org/10.1021/ci960372k.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Knox, 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 (2010): 8255–57. http://dx.doi.org/10.1021/ja102932n.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Gossert, 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 (2011): 210–13. http://dx.doi.org/10.1021/ja108383x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Wei, 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 (2016): 9556–64. http://dx.doi.org/10.1002/chem.201601871.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Karjalainen, 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 (2020): 741–52. http://dx.doi.org/10.1007/s10858-020-00347-5.

Full text

Abstract:

AbstractUnidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T2) relaxation times allowing sophisticated coherence transfer pathway selection in comparison to folded proteins. 1Hα-detection ensures non-susceptibility to chemical exchange with the solvent and enables chemical shift assignment of consecutive proline residues, typically abundant in IDPs. However, many IDPs undergo a disorder-to-order transition upon interaction with their target protein, which leads to the loss of the fa

APA, Harvard, Vancouver, ISO, and other styles

22

Barbet-Massin, Emeline, Andrew J. Pell, Joren S. Retel, et al. "Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning." Journal of the American Chemical Society 136, no. 35 (2014): 12489–97. http://dx.doi.org/10.1021/ja507382j.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Morris, 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 (1985): 1122–28. http://dx.doi.org/10.1016/0006-291x(85)90302-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Lin, 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 (2003): 387–409. http://dx.doi.org/10.1142/s0219720003000083.

Full text

Abstract:

NMR resonance assignment is one of the key steps in solving an NMR protein structure. The assignment process links resonance peaks to individual residues of the target protein sequence, providing the prerequisite for establishing intra- and inter-residue spatial relationships between atoms. The assignment process is tedious and time-consuming, which could take many weeks. Though there exist a number of computer programs to assist the assignment process, many NMR labs are still doing the assignments manually to ensure quality. This paper presents a new computational method based on the combinat

APA, Harvard, Vancouver, ISO, and other styles

25

Hiller, 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 (2007): 10823–28. http://dx.doi.org/10.1021/ja072564+.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Cutting, 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 (2004): 205–10. http://dx.doi.org/10.1023/b:jnmr.0000048947.28598.ea.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Schubert, 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 (2002): 1019–23. http://dx.doi.org/10.1002/1439-7633(20021004)3:10<1019::aid-cbic1019>3.0.co;2-c.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Solyom, 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 (2013): 311–21. http://dx.doi.org/10.1007/s10858-013-9715-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Schmidt, Elena, and Peter Güntert. "Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins." Journal of Biomolecular NMR 57, no. 2 (2013): 193–204. http://dx.doi.org/10.1007/s10858-013-9779-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Shcherbakov, 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 (2020): 193–204. http://dx.doi.org/10.1007/s10858-020-00306-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Kumar, 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 (2010): 111–17. http://dx.doi.org/10.1016/j.jmr.2010.02.013.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Averseng, Olivier, Agnès Hagège, Frédéric Taran, and Claude Vidaud. "Surface Plasmon Resonance for Rapid Screening of Uranyl Affine Proteins." Analytical Chemistry 82, no. 23 (2010): 9797–802. http://dx.doi.org/10.1021/ac102578y.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

LI, 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 (2010): no. http://dx.doi.org/10.1002/chin.199737284.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Romero, 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 (2022): e1010258. http://dx.doi.org/10.1371/journal.pcbi.1010258.

Full text

Abstract:

NMR spectroscopy is key in the study of intrinsically disordered proteins (IDPs). Yet, even the first step in such an analysis—the assignment of observed resonances to particular nuclei—is often problematic due to low peak dispersion in the spectra of IDPs. We show that the assignment process can be aided by finding “hidden” chemical shift patterns specific to the amino acid residue types. We find such patterns in the training data from the Biological Magnetic Resonance Bank using linear discriminant analysis, and then use them to classify spin systems in an α-synuclein sample prepared by us.

APA, Harvard, Vancouver, ISO, and other styles

35

Song, 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 (1988): 8547–48. http://dx.doi.org/10.1021/ja00233a042.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Salzmann, 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 (1998): 13585–90. http://dx.doi.org/10.1073/pnas.95.23.13585.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Feuerstein, 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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Williams, Robert V., Monique J. Rogals, Alexander Eletsky, et al. "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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Löhr, 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 (1995): 189–97. http://dx.doi.org/10.1007/bf00211783.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Medvedeva, 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 (1993): 251–56. http://dx.doi.org/10.1016/0014-5793(93)80664-g.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Löhr, 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 (1996): 259–68. http://dx.doi.org/10.1006/jmrb.1996.0140.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Plevin, 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 (2011): 61–67. http://dx.doi.org/10.1007/s10858-010-9463-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Iuga, 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 (2006): 301–5. http://dx.doi.org/10.1016/j.bbrc.2006.05.116.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Boyko, Kristina V., Erin A. Rosenkranz, Derrick M. Smith, et al. "Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins." PLOS ONE 16, no. 10 (2021): e0258531. http://dx.doi.org/10.1371/journal.pone.0258531.

Full text

Abstract:

A significant number of proteins possess sizable intrinsically disordered regions (IDRs). Due to the dynamic nature of IDRs, NMR spectroscopy is often the tool of choice for characterizing these segments. However, the application of NMR to IDRs is often hindered by their instability, spectral overlap and resonance assignment difficulties. Notably, these challenges increase considerably with the size of the IDR. In response to these issues, here we report the use of sortase-mediated ligation (SML) for segmental isotopic labeling of IDR-containing samples. Specifically, we have developed a ligat

APA, Harvard, Vancouver, ISO, and other styles

45

Jang, 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 (2011): 347–63. http://dx.doi.org/10.1089/cmb.2010.0251.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Zawadzka-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 (2010): 109–16. http://dx.doi.org/10.1016/j.jmr.2009.10.006.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Wen, 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 (2011): 94–100. http://dx.doi.org/10.1016/j.jmr.2010.12.012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Boucher, 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 (1992): 2262–64. http://dx.doi.org/10.1021/ja00032a053.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Stratmann, 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 (2008): 474–81. http://dx.doi.org/10.1093/bioinformatics/btn638.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

McIntosh, 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 (1990): 1–38. http://dx.doi.org/10.1017/s0033583500005400.

Full text

Abstract:

The use of isotopic substitution is a time-honoured method for simplifying the nuclear magnetic resonance spectra of biological macromolecules. For example, the biosynthetic incorporation of a heteronucleus such as15N or13C into a specific amino acid residue in a protein followed by direct observation of the15N or13C NMR spectrum could provide a means to specifically observe a given amino acid type in that protein. By observation of the chemical shift or relaxation properties as a function of pH, ligand concentration, etc. a number of important conclusions concerning the pKavalues of specific

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!