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    Protein Structure Identification Service

      The utilization of the bottom-up approach in proteomics is often constrained by the incomplete characterization of alternatively spliced isoforms, a wide array of post-translational modifications, and native protein degradation. With advancements in analytical technologies, the top-down strategy has gained prominence. Beyond the FT-ICR mass spectrometer, the development and innovative applications of the Orbitrap mass spectrometer have significantly enhanced top-down proteomics.

       

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      Figure 1. Identification of Protein Structure

       

      Since proteins do not require digestion before analysis, employing a top-down strategy can retain and detect information lost when using shotgun methods, such as the quaternary structure containing disulfide bonds. This unique advantage of the top-down approach enables the characterization of disulfide bonds and other post-translational modifications at the protein level. As a result, the top-down method is increasingly applied in QC analyses of protein therapeutics like insulin to assess whether recombinant proteins are correctly expressed, folded, and assembled.

       

      MtoZ Biolabs employs the Thermo Fisher Orbitrap Fusion Lumos mass spectrometry platform combined with nanoLC-MS/MS nanoscale chromatography, providing top-down protein structural characterization services.

       

    • • Protein Primary Structure Characterization Service

      The primary structure of proteins is fundamental to the biological function of proteins, and determining the primary structure aids in studying the function of proteins. MtoZ Biolabs provides protein primary structure detection service based on mass spectrometry.

    • • CE-SDS Protein Isoform Analysis Service

      Protein isoform analysis is a method to study the differences in structure and function of proteins. Proteins are key molecules in life activities, and their functions are closely related to their structures. However, the same amino acid sequence may form multiple different three-dimensional structures, which are called isoforms. Protein isoforms may result from various factors, such as post-translational modifications, heterologous expression, environmental factors, etc.

    • • Protein Circular Dichroism Analysis Service

      Proteins exhibit asymmetric secondary structures such as α-helices, β-sheets, β-turns, and others, leading to differential absorption of left and right circularly polarized light. Upon transmission through these proteins, the circularly polarized light becomes elliptically polarized, a phenomenon known as protein circular dichroism (CD).

    • • Protein Secondary Structure Analysis Service

      Protein secondary structure analysis refers to the study of local spatial structures between continuous amino acid residues in proteins, mainly including α-helix, β-sheet, and others. Understanding protein secondary structures helps reveal their folding mechanisms, stability, function, and interactions with other biomolecules, providing important information for studying the biological functions and regulatory mechanisms of proteins.

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