一般描述
QLAM-AβIδ1LVproR-U-[13C] Kit has 13C isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.
应用
For protein methyl group assignment by 13C isotope labeling of amino acid methyl groups separately or simultaneously.
Using QLAM-AβIδ1LVproR-U-[13C] kit, methyl bearing amino acids like alanine, isoleucine, leucine and valine are labeled with 13C isotopomer. This kit has been tested with protein isotopic labeling in E. coli. It is also used to provide good coverage across the structure of membrane proteins and information of structural dynamics and interactions in solid-state NMR spectroscopy.
包装
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.
Vilius Kurauskas et al.
Methods in molecular biology (Clifton, N.J.), 1635, 109-123 (2017-07-30)
Methyl groups are very useful probes of structure, dynamics, and interactions in protein NMR spectroscopy. In particular, methyl-directed experiments provide high sensitivity even in very large proteins, such as membrane proteins in a membrane-mimicking environment. In this chapter, we discuss
Maggy Hologne et al.
Journal of the American Chemical Society, 127(32), 11208-11209 (2005-08-11)
We show in this communication that dynamic information for uniformly 2H,13C,15N isotopically enriched, crystalline proteins can be obtained by MAS solid-state NMR spectroscopy. The experiments make use of the deuterium quadrupolar tensor, which is the dominant interaction mechanism. Dynamic properties
Rime Kerfah et al.
Journal of biomolecular NMR, 63(4), 389-402 (2015-11-15)
A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back (13)C-(13)C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has
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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