BioNMR Promo

Understanding Function by Solving Protein Structure

If you're analyzing proteins,
you must consider...

Uniform Labeling (click here)
via biosynthetic incorporation of stable isotopes into all carbon, nitrogen and/or hydrogen sites by growing bacteria in minimal media (D-Glucose-¹³C₆, ¹⁵NH₄Cl, D₂O) or by utilizing our complex growth media ISOGRO^®. Open up many avenues for NMR studies of proteins and make assignments by comparisons with spectra from selectively labeled samples.

Selective Labeling (click here) via biosynthetic incorporation of a single type of labeled amino acid. This is used to assist resonance assignments in both solution NMR and solid-state NMR experiments since only the signals from the labeled sites are observed. This tool in conjunction with uniform labeling is extremely valuable in aiding protein structure determination.

Selective Methyl Labeling
(click here) in key protein structures permits high sensitivity and resolution for determination of global folds in larger proteins. Alpha-ketoacids serve for incorporating methyl moieties resulting in desired isotopic labeling patterns of proteins expressed in minimal media. Additional applications include studying protein-ligand interactions and high throughput screening of ligands to larger proteins.

Cell-Free Protein Synthesis (click here) Protein expression systems in living cells can have various limitations such as toxicity, solubility, and the presence of proteases. Cell Free synthesis utilizes the cell’s translation and/or transcription system to synthesize proteins in vitro. By utilizing this method, uniform and site directed stable isotope labeled proteins can be prepared.

...if you want this.