Reveal details of your peptide in solids and liquids
Nuclear Magnetic Resonance (NMR) spectroscopy is one of the most robust and versatile tools in modern analytical science, especially in peptide and protein analysis. At Triclinic Labs, we specialize in comprehensive NMR-based investigations to elucidate peptides' structure, dynamics, and interactions in solution and solid-state environments. Whether you aim to understand a peptide’s biological function, confirm synthesis, or investigate interactions with other biomolecules, our advanced instrumentation and experienced scientists provide the necessary insights you need.
We offer the following peptide analysis services using NMR:
- Structural Characterization
- Determine primary and secondary structures of peptides.
- Identify backbone and side-chain interactions using chemical shift assignments.
- Conformational Analysis
- Study the effects of solvents, pH, temperature, and ligand binding on conformation.
- Peptide Dynamics and Interactions
- Monitor molecular motion and flexibility through relaxation time measurements.
- Study peptide-protein, peptide-lipid, and peptide-drug interactions.
- Quantitative Analysis
- Determine peptide purity and concentration.
NMR Experiments Offered at Triclinic Labs:
- 1D NMR (1H, 13C, 15N, 19F, 31P, etc.): Basic structural information and purity check.
- COSY (Correlation Spectroscopy): Identifies adjacent protons in amino acid side chains and backbone.
- TOCSY (Total Correlation Spectroscopy): Assigns entire spin systems (e.g., all protons within an amino acid residue).
- NOESY (Nuclear Overhauser Effect Spectroscopy): Provides through-space interactions (< 5-6 Å) between protons.
- HSQC(Heteronuclear Single Quantum Coherence): Correlates protons with directly bonded heteronuclei (e.g., ¹H-¹³C or ¹H-¹⁵N).
- HMBC (Heteronuclear Multiple Bond Correlation): Identifies long-range 1H-13C or 1H-15N couplings, often used for side-chain assignments in peptides.
- T1 (Longitudinal Relaxation) and T2 (Transverse Relaxation) analyses: Probes hydration (e.g., water-protein interactions) and dynamics (e.g., folded vs. disordered).
- DOSY (Diffusion-Ordered Spectroscopy): Examines size, aggregates, ligand binding, and mixture resolution.
Requirements for Successful Peptide NMR Analysis
- Sample Preparation
- High-purity peptide (typically >95%) or isotopically labeled peptides to avoid spectral contamination.
- Proper solvent selection to minimize background signals (e.g., deuterated solvents like D2O or PBS in D2O). It is critical to determine the best solvent system and concentration.
- pH adjustment influences chemical shifts and peptide folding.
- Appropriate concentration (typically 0.1-5 mM) to optimize signal-to-noise ratio without causing aggregation.
- NMR Instrumentation
- Triclinic uses High-field NMR spectrometers (400-900 MHz) to enhance resolution and sensitivity.
- Triple-resonance cryoprobes improve signal detection, especially for low-concentration samples.
- Isotopic Labeling (for Large Peptides or Proteins)
- 13C and 15N labeling helps assign individual nuclei in large peptides.
- Deuterium (²H) labeling improves spectral resolution by reducing peak overlap.
- Standardizing and Annotating Protein NMR Chemical Shift DataChemical shift referencing and assignment using the Biological Magnetic Resonance Bank (BMRB)
At Triclinic Labs, our experience with complex peptide systems, state-of-the-art instrumentation, and a
rigorous analytical approach allows us to deliver actionable insights with precision and reliability. Our
services are fully customizable, whether you're in drug discovery, formulation development, quality
assurance, or academic research.
Let us help you unlock the full potential of your peptides through expert NMR analysis.
