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Dynamic and Conformational Study Service for Proteins Based on 800 MHz Spectrometer

STEMart offers advanced Dynamic and Conformational Study Services for proteins, utilizing our cutting-edge 800 MHz spectrometers, including the Bruker Avance III HD 800 MHz and JEOL ECA 800 MHz systems. These high-frequency instruments provide the precision and sensitivity required to study complex protein dynamics and structural conformations. Our services empower researchers with detailed insights into protein flexibility, folding, and structural rearrangements, essential for understanding protein function and stability

Our 800 MHz NMR spectrometers work on nuclear magnetic resonance principles, capturing dynamic changes in protein structure at atomic resolution. Through specialized techniques such as Nuclear Overhauser Effect Spectroscopy (NOESY), relaxation measurements, and temperature-dependent NMR, we provide real-time insights into protein behavior and conformation. This technology is extensively applied in fields like structural biology, drug discovery, and biophysics to reveal how proteins interact, fold, and respond to environmental changes

Leveraging our high-performance 800 MHz NMR systems, STEMart offers a comprehensive range of dynamic and conformational studies, including folding analysis, ligand-induced conformational changes, and relaxation studies. Our services are designed to deliver robust, high-quality data to support researchers in elucidating protein mechanisms and enhancing therapeutic development

What We Offer

  • Protein Folding and Unfolding Analysis

Detailed analysis of protein folding pathways and stability, helping researchers understand the molecular basis of folding diseases and protein function.

  • Conformational Changes upon Ligand Binding

Studies the conformational shifts in proteins induced by ligand interactions, essential for drug discovery and understanding protein-ligand binding mechanisms.

  • Relaxation Measurements for Dynamics Studies

Provides relaxation analysis to quantify protein motion, offering insights into protein flexibility and function at various timescales.

  • Temperature-Dependent NMR Studies

Monitors structural changes across temperature gradients, supporting stability and conformational studies relevant to protein engineering and drug formulation

Why Choose Us

  • High Sensitivity for Detecting Conformational Changes

Our 800 MHz NMR spectrometers offer unmatched sensitivity, ideal for capturing subtle conformational shifts and dynamic protein behavior.

  • Expert NMR Team in Protein Dynamics

Our team has specialized expertise in protein dynamics, providing reliable data interpretation to advance structural and functional research.

  • Flexible Reporting for Tailored Insights

We provide customizable reports to suit specific research needs, ensuring clear and actionable data presentation.

  • Non-Invasive Analysis in Solution

Our solution-based NMR methods allow proteins to be studied in near-physiological conditions, preserving native conformations for accurate insights

Our Resources

Bruker Avance III HD 800 MHz NMR

The Bruker Avance III HD 800 MHz spectrometer, equipped with Cryoprobe technology, offers high resolution and sensitivity for protein dynamics studies. Its advanced capabilities support detailed analysis of conformational changes, essential for studying protein-ligand interactions and structural flexibility

JEOL ECA 800 MHz NMR

This 800 MHz spectrometer from JEOL provides robust performance for examining protein dynamics and conformation. Its precision and sensitivity enable accurate measurements, making it ideal for studies involving protein folding, relaxation measurements, and ligand-induced conformational changes

STEMart provides high-quality NMR services tailored to meet the specific needs of our clients. Our experienced specialists use advanced equipment and follow strict quality control measures to ensure accurate and reliable results. Contact us to learn more about our NMR services and how we can help you achieve your research goals.

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