 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
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| MeSH Number(s) |
E05.196.867.519.550
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| Concept/Terms |
Protein NMR Spectroscopy- Protein NMR Spectroscopy
- NMR Spectroscopy, Protein
- NMR Spectroscopies, Protein
- Protein NMR Spectroscopies
- Spectroscopies, Protein NMR
- Spectroscopy, Protein NMR
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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 |
|---|
| 1995 | 0 | 1 | 1 | | 1997 | 0 | 3 | 3 | | 1998 | 0 | 6 | 6 | | 1999 | 2 | 3 | 5 | | 2000 | 1 | 2 | 3 | | 2001 | 3 | 3 | 6 | | 2002 | 0 | 9 | 9 | | 2003 | 1 | 5 | 6 | | 2004 | 2 | 8 | 10 | | 2005 | 2 | 6 | 8 | | 2006 | 1 | 8 | 9 | | 2007 | 2 | 6 | 8 | | 2008 | 2 | 6 | 8 | | 2009 | 1 | 13 | 14 | | 2010 | 6 | 11 | 17 | | 2011 | 0 | 12 | 12 | | 2012 | 2 | 4 | 6 | | 2013 | 4 | 8 | 12 | | 2014 | 2 | 9 | 11 | | 2015 | 2 | 6 | 8 | | 2016 | 2 | 9 | 11 | | 2017 | 3 | 6 | 9 | | 2018 | 4 | 7 | 11 | | 2019 | 1 | 5 | 6 |
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Below are the most recent publications written about "Nuclear Magnetic Resonance, Biomolecular" by people in Profiles.
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Vugmeyster L, Au DF, Ostrovsky D, Fu R. Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-ß Fibrils. Chemphyschem. 2019 07 02; 20(13):1680-1689.
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Zhang Y, Jang Y, Lee JE, Ahn J, Xu L, Holden MR, Cornett EM, Krajewski K, Klein BJ, Wang SP, Dou Y, Roeder RG, Strahl BD, Rothbart SB, Shi X, Ge K, Kutateladze TG. Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF. Nat Commun. 2019 05 24; 10(1):2314.
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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 ßa protein. Proc Natl Acad Sci U S A. 2019 04 02; 116(14):6806-6811.
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Au DF, Ostrovsky D, Fu R, Vugmeyster L. Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-ß fibrils. J Biol Chem. 2019 04 12; 294(15):5840-5853.
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Jones DNM, Wang J, Murphy EJ. Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid. Biomol NMR Assign. 2019 04; 13(1):187-193.
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Zhang S, Zhang Y, Stenzoski NE, Zou J, Peran I, McCallum SA, Raleigh DP, Royer CA. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates. Biophys J. 2019 02 05; 116(3):445-453.
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Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. PLoS Biol. 2019 01; 17(1):e3000100.
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Born A, Nichols PJ, Henen MA, Chi CN, Strotz D, Bayer P, Tate SI, Peng JW, Vögeli B. Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery. Biomol NMR Assign. 2019 04; 13(1):85-89.
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Shah DD, Singh SM, Mallela KMG. Effect of Chemical Oxidation on the Higher Order Structure, Stability, Aggregation, and Biological Function of Interferon Alpha-2a: Role of Local Structural Changes Detected by 2D NMR. Pharm Res. 2018 Oct 15; 35(12):232.
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Wall KP, Hough LE. In-Cell NMR within Budding Yeast Reveals Cytoplasmic Masking of Hydrophobic Residues of FG Repeats. Biophys J. 2018 11 06; 115(9):1690-1695.
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