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DLAM-LVproS-13CHD2 Methyl Labeling Kit

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technique(s)

bio NMR: suitable

Quality Level

shipped in

dry ice

storage temp.

−70°C

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This Item
906573906611906581
storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

General description

DLAM-LVproS-13CHD2 kit has 13CHD2 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.

Application

DLAM-LVproS-13CHD2 kit is used for double labeling of amino acid precursors, leucine and valine with 13CHD2 isotopomer. This kit has been tested with protein isotopic labeling in E. coli. Stereospecific incorporation of 13CHD2 groups in perdeuterated proteins allows for the measurement of precise dynamics information and the acquisition of high resolution 1H,13C-spectra by solution and solid-state NMR spectroscopy.
For solid-state NMR applications and dynamic studies.
For regio- and/or stereo- specific isotope labelilng of Isoleucine, Leucine, Valine, and Alanine with 13CHD2 isotopomers.

Packaging

This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.

Storage Class Code

11 - Combustible Solids


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Rime Kerfah et al.
Current opinion in structural biology, 32, 113-122 (2015-04-17)
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting
Silke Wiesner et al.
Current opinion in structural biology, 35, 60-67 (2015-09-26)
Intermolecular interactions are indispensible for biological function. Here we discuss how novel NMR techniques can provide unique insights into the assembly, dynamics and regulation of biomolecular complexes. We focus on applications that exploit the methyl TROSY effect and show that

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