906506
HLAM-AβIδ1MεLVproSTγ-13CH3 Methyl Labeling Kit
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About This Item
Codice UNSPSC:
12352200
NACRES:
NA.12
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tecniche
bio NMR: suitable
Livello qualitativo
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Descrizione generale
HLAM-AβIδ1MεLVproSTγ-13CH3 kit has 13CH3 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.
Applicazioni
For detection of long-range nOes or for the NMR study of large proteins
HLAM-AβIδ1MεLVproSTγ-13CH3 is an optimized kit used to produce proteins with 13CH3 isotopomer on methyl groups of alanine, isoleucine, methionine, leucine and threonine residues. This kit has been tested with protein isotopic labeling in E. coli. It can be used to study large molecular system and complex protein structure in NMR spectroscopy along with other spectroscopic approaches. The sensitivity of the isotopomer can be enhanced by three-fold multiplicity. This kit can also be used to simplify crowded spectra to provide specific probes of dynamic and structural studies in solid state NMR spectroscopy.
Confezionamento
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. jj
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César Fernández et al.
Current opinion in structural biology, 13(5), 570-580 (2003-10-22)
Transverse relaxation-optimized spectroscopy (TROSY), in combination with various isotope-labeling techniques, has opened avenues to study biomolecules with molecular masses of up to 1000000Da by solution NMR. Important recent applications of TROSY include the structure determination of membrane proteins in detergent
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
Articoli
Methyl Isotope-Labeling of Proteins from NMR-Bio
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