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 | 4 | 5 |
| 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 |
| 2020 | 0 | 1 | 1 |
| 2021 | 1 | 0 | 1 |
| 2022 | 0 | 1 | 1 |
| 2024 | 1 | 0 | 1 |
| 2025 | 2 | 0 | 2 |
| 2026 | 1 | 1 | 2 |
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Below are the most recent publications written about "Nuclear Magnetic Resonance, Biomolecular" by people in Profiles.
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Bhasne K, D?rries L, Maqtedar A, Mager ST, Clerico EM, Gierasch LM. Model Peptides Enable Comparisons of Substrate Binding Modes of Hsp70 Molecular Chaperones. Biochemistry. 2026 Apr 21; 65(8):1214-1223.
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Xie H, Zhao W, Xiao H, Zhang Y, Shen Y, Gan Y, Tong Q, Zhao Y, Tan H, Yang J. In Situ Structure Determination of a Membrane Protein in E. coli Cellular Membranes by Proton-Detected Solid-State NMR. J Am Chem Soc. 2026 Mar 11; 148(9):9433-9448.
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Kuzio NJ, Tonelli M, Fejzo J, Hardy JA. An NMR sample preparation case study: Considerations for the self-destructive protease caspase-6. PLoS One. 2025; 20(11):e0337291.
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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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Afek A, Shi H, Rangadurai A, Sahay H, Senitzki A, Xhani S, Fang M, Salinas R, Mielko Z, Pufall MA, Poon GMK, Haran TE, Schumacher MA, Al-Hashimi HM, Gord?n R. DNA mismatches reveal conformational penalties in protein-DNA recognition. Nature. 2020 11; 587(7833):291-296.
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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.