NMR-Based Methods for Protein Analysis
- PMID: 33439619
- DOI: 10.1021/acs.analchem.0c03830
NMR-Based Methods for Protein Analysis
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special emphasis on in-cell protein structural determination and the analysis of protein dynamics, both difficult to be accessed by traditional methods.
Similar articles
-
Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.J Biol Chem. 2019 Nov 1;294(44):15914-15931. doi: 10.1074/jbc.REV119.009178. Epub 2019 Sep 24. J Biol Chem. 2019. PMID: 31551353 Free PMC article. Review.
-
Structures of Large Protein Complexes Determined by Nuclear Magnetic Resonance Spectroscopy.Annu Rev Biophys. 2017 May 22;46:317-336. doi: 10.1146/annurev-biophys-070816-033701. Epub 2017 Mar 17. Annu Rev Biophys. 2017. PMID: 28375736 Review.
-
In situ structural biology using in-cell NMR.Biochim Biophys Acta Gen Subj. 2020 Feb;1864(2):129364. doi: 10.1016/j.bbagen.2019.05.007. Epub 2019 May 16. Biochim Biophys Acta Gen Subj. 2020. PMID: 31103749 Review.
-
Beyond detergent micelles: The advantages and applications of non-micellar and lipid-based membrane mimetics for solution-state NMR.Prog Nucl Magn Reson Spectrosc. 2019 Oct-Dec;114-115:271-283. doi: 10.1016/j.pnmrs.2019.08.001. Epub 2019 Aug 26. Prog Nucl Magn Reson Spectrosc. 2019. PMID: 31779883 Review.
-
New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.J Mol Biol. 2016 Jan 29;428(2 Pt A):323-331. doi: 10.1016/j.jmb.2015.11.028. Epub 2015 Dec 19. J Mol Biol. 2016. PMID: 26707200 Review.
Cited by
-
In situ characterization of amine-forming enzymes shows altered oligomeric state.Protein Sci. 2025 Jan;34(1):e5248. doi: 10.1002/pro.5248. Protein Sci. 2025. PMID: 39720905 Free PMC article.
-
Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Adv Sci (Weinh). 2025 May;12(19):e2414777. doi: 10.1002/advs.202414777. Epub 2025 Mar 24. Adv Sci (Weinh). 2025. PMID: 40125621 Free PMC article.
-
Unfolding of the Villin Headpiece Domain: Revealing Structural Heterogeneity with Time-Resolved X-Ray Solution Scattering and Markov State Modeling.Chemphyschem. 2025 Jun 23;26(12):e202500049. doi: 10.1002/cphc.202500049. Epub 2025 May 20. Chemphyschem. 2025. PMID: 40192555 Free PMC article.
-
Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins. 2025 Aug;93(8):1314-1329. doi: 10.1002/prot.26561. Epub 2023 Aug 2. Proteins. 2025. PMID: 37530227 Free PMC article. Review.
-
Structure Modeling Protocols for Protein Multimer and RNA in CASP16 With Enhanced MSAs, Model Ranking, and Deep Learning.Proteins. 2025 Aug 1:10.1002/prot.70033. doi: 10.1002/prot.70033. Online ahead of print. Proteins. 2025. PMID: 40751131
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous