Nuclear Magnetic Resonance, Biomolecular
"Nuclear Magnetic Resonance, Biomolecular" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.
| Descriptor ID |
D019906
|
| MeSH Number(s) |
E05.196.867.519.550
|
| Concept/Terms |
Protein NMR Spectroscopy- Protein NMR Spectroscopy
- NMR Spectroscopy, Protein
- NMR Spectroscopies, Protein
- Protein NMR Spectroscopies
- Spectroscopies, Protein NMR
- Spectroscopy, Protein NMR
|
Below are MeSH descriptors whose meaning is more general than "Nuclear Magnetic Resonance, Biomolecular".
Below are MeSH descriptors whose meaning is more specific than "Nuclear Magnetic Resonance, Biomolecular".
This graph shows the total number of publications written about "Nuclear Magnetic Resonance, Biomolecular" by people in this website by year, and whether "Nuclear Magnetic Resonance, Biomolecular" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1997 | 0 | 1 | 1 |
| 1998 | 0 | 1 | 1 |
| 1999 | 0 | 1 | 1 |
| 2000 | 0 | 4 | 4 |
| 2001 | 0 | 3 | 3 |
| 2002 | 0 | 8 | 8 |
| 2003 | 0 | 18 | 18 |
| 2004 | 1 | 4 | 5 |
| 2005 | 0 | 4 | 4 |
| 2006 | 1 | 5 | 6 |
| 2007 | 2 | 1 | 3 |
| 2008 | 0 | 5 | 5 |
| 2009 | 0 | 3 | 3 |
| 2010 | 0 | 8 | 8 |
| 2011 | 2 | 5 | 7 |
| 2012 | 1 | 3 | 4 |
| 2013 | 0 | 6 | 6 |
| 2014 | 0 | 4 | 4 |
| 2015 | 0 | 1 | 1 |
| 2016 | 0 | 2 | 2 |
| 2017 | 0 | 1 | 1 |
| 2018 | 1 | 2 | 3 |
| 2019 | 1 | 1 | 2 |
| 2021 | 1 | 0 | 1 |
| 2022 | 0 | 1 | 1 |
| 2024 | 1 | 0 | 1 |
| 2025 | 1 | 0 | 1 |
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Below are the most recent publications written about "Nuclear Magnetic Resonance, Biomolecular" by people in Profiles.
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Xiao H, Wang J, Tan H, Gan Y, Liu W, Zhang Y, Zhang Z, Yang J. Robust Heteronuclear Correlations for Sub-milligram Protein in Ultrafast Magic-Angle Spinning Solid-State NMR. J Am Chem Soc. 2025 Feb 26; 147(8):6384-6389.
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Xiao H, Zhao W, Zhang Y, Kang H, Zhang Z, Yang J. Selective correlations between aliphatic 13C nuclei in protein solid-state NMR. J Magn Reson. 2024 Aug; 365:107730.
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Zhang Z, Su Y, Xiao H, Yang J. Selective Nuclear Magnetic Resonance Method for Enhancing Long-Range Heteronuclear Correlations in Solids. J Phys Chem Lett. 2022 Jul 14; 13(27):6376-6382.
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Xiao H, Zhang Z, Zhao Y, Yang J. Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR. J Biomol NMR. 2021 May; 75(4-5):193-202.
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Ishima R, Kurt Yilmaz N, Schiffer CA. NMR and MD studies combined to elucidate inhibitor and water interactions of HIV-1 protease and their modulations with resistance mutations. J Biomol NMR. 2019 Jul; 73(6-7):365-374.
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Basak S, Nobrega RP, Tavella D, Deveau LM, Koga N, Tatsumi-Koga R, Baker D, Massi F, Matthews CR. Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed ?a protein. Proc Natl Acad Sci U S A. 2019 04 02; 116(14):6806-6811.
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Spronk CAEM, Zerko S, G?rka M, Kozminski W, Bardiaux B, Zambelli B, Musiani F, Piccioli M, Basak P, Blum FC, Johnson RC, Hu H, Merrell DS, Maroney M, Ciurli S. Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools. J Biol Inorg Chem. 2018 12; 23(8):1309-1330.
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Tavella D, Zitzewitz JA, Massi F. Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis. Biophys J. 2018 11 06; 115(9):1673-1680.
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Khan SN, Persons JD, Paulsen JL, Guerrero M, Schiffer CA, Kurt-Yilmaz N, Ishima R. Probing Structural Changes among Analogous Inhibitor-Bound Forms of HIV-1 Protease and a Drug-Resistant Mutant in Solution by Nuclear Magnetic Resonance. Biochemistry. 2018 03 13; 57(10):1652-1662.
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Lai AL, Clerico EM, Blackburn ME, Patel NA, Robinson CV, Borbat PP, Freed JH, Gierasch LM. Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance. J Biol Chem. 2017 05 26; 292(21):8773-8785.