Related ArticlesRecent advances in protein NMR spectroscopy and their implications in protein therapeutics research.
Anal Bioanal Chem. 2013 Dec 6;
Authors: Wang G, Zhang ZT, Jiang B, Zhang X, Li C, Liu M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography are the two main methods for protein three-dimensional structure determination at atomic resolution. According to the protein structures deposited in the Protein Data Bank, X-ray crystallography has become the dominant method for structure determination, particularly for large proteins and complexes. However, with the developments of isotope labeling, increase of magnetic field strength, common use of a cryogenic probe, and ingenious pulse sequence design, the applications of NMR spectroscopy have expanded in biological research, especially in characterizing protein dynamics, sparsely populated transient structures, weak protein interactions, and proteins in living cells at atomic resolution, which is difficult if not impossible by other biophysical methods. Although great advances have been made in protein NMR spectroscopy, its applications in protein therapeutics, which represents the fastest growing segment of the pharmaceutical industry, are still limited. Here we review the recent advances in the use of NMR spectroscopy in studies of large proteins or complexes, posttranslation modifications, weak interactions, and aggregation, and in-cell NMR spectroscopy. The potential applications of NMR spectroscopy in protein therapeutic assays are discussed.
PMID: 24309626 [PubMed - as supplied by publisher]
[NMR paper] Recent advances in computational predictions of NMR parameters for the structure elucidation of carbohydrates: methods and limitations.
Recent advances in computational predictions of NMR parameters for the structure elucidation of carbohydrates: methods and limitations.
Related Articles Recent advances in computational predictions of NMR parameters for the structure elucidation of carbohydrates: methods and limitations.
Chem Soc Rev. 2013 Jul 25;
Authors: Toukach FV, Ananikov VP
Abstract
All living systems are comprised of four fundamental classes of macromolecules - nucleic acids, proteins, lipids, and carbohydrates (glycans). Glycans play a unique role of joining three...
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07-28-2013 07:46 PM
[NMR paper] Recent applications of isotopic labeling for protein NMR in drug discovery.
Recent applications of isotopic labeling for protein NMR in drug discovery.
Related Articles Recent applications of isotopic labeling for protein NMR in drug discovery.
Expert Opin Drug Discov. 2013 Mar 12;
Authors: Hiroaki H
Abstract
Introduction: Nuclear magnetic resonance (NMR) applications in drug discovery are classified into two categories: ligand-based methods and protein-based methods. The latter is based on the observation of the (1)H-(15)N HSQC spectra of a protein with and without lead compounds. However, in order to take this...
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03-14-2013 10:05 PM
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
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09-08-2011 06:50 PM
Advances in automated NMR protein structure determination.
Advances in automated NMR protein structure determination.
Advances in automated NMR protein structure determination.
Q Rev Biophys. 2011 Mar 17;:1-53
Authors: Guerry P, Herrmann T
Around half of all protein structures solved nowadays using solution-state nuclear magnetic resonance (NMR) spectroscopy have been because of automated data analysis. The pervasiveness of computational approaches in general hides, however, a more nuanced view in which the full variety and richness of the field appears. This review is structured around a comparison of...
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03-18-2011 06:00 PM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.
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