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    Therapeutics Characterization Service | Advanced Structural

      • • Disulfide Bond Mapping Analysis Service

        Disulfide bonds are a crucial structural element in proteins, formed by the sulfur atoms from cysteine amino acid residues under oxidative conditions. These bonds play a pivotal role in the biological activity and functionality of proteins. Found extensively in proteins such as cellular surface receptors, antibodies, growth factors, hormones, and enzymes, disulfide bonds are prone to reduction or mispairing, impacting the structure and biological activity of the originating peptides or proteins.

      • • Differential Scanning Calorimetry (DSC) Analysis Service

        Thermal stability is defined as the ability of a substance to resist irreversible chemical or physical changes at elevated temperatures, typically by preventing decomposition or polymerization. This property is particularly important in some proteins. In proteins that are sensitive to high temperatures, increased heat can disrupt the intramolecular bonds within their tertiary and quaternary structures, leading to protein unfolding and inactivation. Therefore, assessing the thermal stability of protein......

      • • FT-IR for Protein and Peptide Analysis Service

        Fourier transform infrared (FT-IR) spectroscopy is a powerful technique for obtaining the infrared spectra of absorption/emission in solids, liquids, or gases. When infrared radiation passes through a test sample, a part of the infrared radiation is absorbed by specific covalent bonds of functional groups, while another part of the infrared radiation directly penetrates through.

      • • Dynamic Light Scattering (DLS) Analysis Service

        Dynamic light scattering (DLS), also known as photon correlation spectroscopy (PCS) or quasi-elastic light scattering (QELS), is a prevalent analytical technique for determining particle sizes and distribution in suspensions or polymer solutions.

      • • Free Sulfhydryl Quantification Service

        Sulfhydryl and disulfide bonds often participate in enzymatic catalysis, cofactor binding, and maintenance of protein active conformations in the form of active functional groups. Analyzing the quantity and characteristics of sulfhydryl groups constitutes a critical method for acquiring specific structural insights in contemporary biochemistry and molecular biology.

      • • Hydrogen Deuterium Exchange Mass Spectrometry, HDX MS Service

        Hydrogen deuterium exchange mass spectrometry (HDX MS) represents a sophisticated technique in mass spectrometry for investigating the spatial conformation of proteins, extensively employed across academia and the biopharmaceutical industry for the analysis of protein structures.

      • • Circular Dichroism (CD) Spectrum Analysis Service

        In recent years, with the progress in the field of drug discovery, circular dichroism (CD) has become one of the core technologies for protein and peptide drug development and research. Circular dichrographic scanning analysis of proteins and peptides is of great significance for studying their secondary and advanced structures.

      • • Disulfide Bond Analysis Service

        MtoZ Biolabs has developed a high-resolution mass spectrometry, coupled with pLink-SS software, to provide our customers with accurate analysis of disulfide bonds and free cysteines.

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