Biomolecular NMR
Isotope-labeled tools for structural and dynamic studies of proteins, RNA, and DNA
Nuclear magnetic resonance (NMR) spectroscopy provides information regarding the structure and dynamics of proteins, RNA, and DNA at the atomic level. These biomolecules may be studied individually or in the presence of ligands or other biomolecules — vital for rational drug design and for expanding knowledge in mechanistic biology.
Biomolecular NMR refers to the use of NMR to study biological compounds in vivo, or under conditions that best mimic in vivo environments. Most cytosolic proteins are relatively easy to study, but membrane proteins require lipophilic environments for stability and function, and are typically studied in micelles, lipid bilayers, cellular membranes, and living cells.
NMR generally lacks the sensitivity to detect useful signals from unlabeled samples, so biomolecules are often enriched in 13C and/or 15N for analysis. Deuterium is often incorporated to simplify spectra or alter relaxation effects, so the necessary spectroscopic information can be acquired. Over the years, advances in isotope-labeling strategies have expanded the size of macromolecules and the depth of detail available for study.
Discover our Biomolecular NMR range →
Related Applications
Methyl and Amino Acid-Type Labeling
Selective labeling strategies that highlight specific residues, simplifying spectra for large macromolecular complexes.
Sparse Labeling for Protein NMR
Reduced-density labeling patterns that lower spectral crowding while preserving key structural information.
Hyperpolarization
Techniques that boost NMR signal intensity, enabling detection of low-concentration or transient species.
In Vivo Protein Expression
Isotope-labeled growth media and reagents for expressing labeled proteins directly in living cells.
Membrane Proteins
Labeling solutions adapted to the lipophilic environments membrane proteins require for stability and function.
MRI/MRS
Isotope-enriched compounds supporting magnetic resonance imaging and spectroscopy research.
Key Isotope Labeling Strategies
- 13C / 15N enrichment — uniform or selective labeling to boost NMR sensitivity and resolve complex spectra.
- Deuteration — simplifies spectra and alters relaxation properties, extending the size range of macromolecules that can be studied.
- Residue-specific labeling — methyl and amino acid-type labeling for targeted structural information in large complexes.
- Sparse labeling — reduced-density schemes that minimize spectral crowding while retaining key structural data.
