Related ArticlesReview of Methods to Assign the NMR Peaks of Reductively Methylated Proteins.
Anal Biochem. 2014 Aug 28;
Authors: Roberson KJ, Macnaughtan MA
Abstract
Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification; first, as a tool to aid protein crystallization and later, as a probe in protein nuclear magnetic resonance (NMR) spectroscopy. As an isotope-labeling strategy for NMR studies, reductive methylation has contributed to the study of protein-protein interactions and global conformational changes. While more detailed structural studies using this labeling strategy are possible, the hurdle of assigning the NMR peaks to the corresponding reductively methylated amine hinders its use. In this review, we discuss and compare strategies used to assign the NMR peaks of reductively methylated protein-amines.
PMID: 25175010 [PubMed - as supplied by publisher]
Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins
Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins
Publication date: Available online 28 August 2014
Source:Analytical Biochemistry</br>
Author(s): Kevin J. Roberson , Megan A. Macnaughtan</br>
Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification; first, as a tool to aid protein crystallization and later, as a probe in protein nuclear magnetic resonance (NMR)...
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08-29-2014 05:36 PM
[NMR paper] Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins.
Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins.
Related Articles Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins.
J Vis Exp. 2013;(82)
Authors: Roberson KJ, Brady PN, Sweeney MM, Macnaughtan MA
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a proven technique for protein structure and dynamic studies. To study proteins with NMR, stable magnetic isotopes are typically incorporated metabolically to...
[NMR900 blog] Review in Nature Methods
Review in Nature Methods
J.R. Bothe, E.N. Nikolova, C.D. Eichhorn, J. Chugh, A.L. Hansen and H.M. Al-Hashimi, "Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy," Nature Methods 8 (2011) 919–931. (Review) http://dx.doi.org/10.1038/nmeth.1735
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11-02-2011 02:14 AM
Using NMR Spectroscopic Methods to Determine Enantiomeric Purity and Assign Absolute
Using NMR Spectroscopic Methods to Determine Enantiomeric Purity and Assign Absolute Stereochemistry
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 2 August 2010</br>
Thomas J., Wenzel , Cora D., Chisholm</br>
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