Biomolecular NMR
Nuclear magnetic resonance (NMR) spectroscopy provides information regarding the structure and dynamics for protein, RNA and DNA at the atomic level. These biomolecules may be studied individually or in the presence of ligands or other biomolecules. Determination of the three-dimensional structure of macromolecules and their complexes is vital for rational drug design and expanding knowledge within the field of mechanistic biology. The term “biomolecular NMR” refers to the use of NMR to study biological compounds in vivo or under conditions which best mimic in vivo conditions. Although most cytosolic proteins are relatively easy to study, membrane proteins require lipophilic environments for stability and function and thus are typically studied in micelles, lipid bilayers, cellular membranes and living cells. NMR generally lacks the sensitivity to detect useful signals from unlabeled sample, therefore biomolecules are often required to be enriched in 13C and/or 15N for analyses. Deuterium is often incorporated to simplify spectra or to alter relaxation effects so that the necessary spectroscopic information may be acquired. Over the years, advances in isotope-labeling strategies have expanded the size of macromolecules and the types of detailed information available for study.

In vivo Protein Expression
Reagents and media for prokaryotic and eukaryotic protein expression
In situ Protein Expression
Reagents and kits for cell-free synthesis
Sparse Labeling for Protein NMR
Sparse13C reagents and media
Membrane Proteins
Deuterated lipids and detergents
Methyl and Amino Acid Type Labeling
Alpha-keto acids and amino acids
Nucleic Acid Synthesis
rNTPs, dNTPs, deoxyphosphoramidites
Protein Standards
Labeled protein supplied in solution and other forms
Hyperpolarization/MRI/MRS
13C substrates for DNP and PHIP