Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of Protein Primary Structure Characterization

  Protein primary structure refers to the linear sequence of amino acids in a protein molecule, which determines the protein's three-dimensional structure and function. Therefore, accurately characterizing the primary structure of proteins is crucial for understanding their function and mechanism. The following is the standard workflow for protein primary structure characterization:

• • Mechanism of Protein Circular Dichroism

  Protein Circular Dichroism (CD) is a critical spectroscopic technique extensively used to investigate protein secondary structures. By measuring the differential absorption of left- and right-circularly polarized light by protein samples, CD spectroscopy offers valuable insights into protein conformation.

• • Principle of Protein Primary Structure Characterization

  Proteins are one of the most crucial functional molecules in living organisms, and their functional diversity primarily stems from their structural complexity. The structure of proteins is divided into four levels: primary, secondary, tertiary, and quaternary structures. The primary structure of a protein refers to its amino acid sequence, which is a linear chain formed by amino acids connected by peptide bonds in a specific order.

• • Application of Protein Circular Dichroism

  Protein Circular Dichroism (CD) is a spectroscopic technique that investigates molecular structures by measuring the differential absorption of circularly polarized light at various wavelengths. Given the chiral nature of protein structures, CD is instrumental in protein research.

• • Workflow of Protein Circular Dichroism

  Protein Circular Dichroism (CD) is an essential spectroscopic technique used to study protein secondary structure and dynamics. By measuring the differential absorption of circularly polarized light at various wavelengths, CD spectra provide information on the α-helix, β-sheet, and random coil structures of proteins.

• • Advantages and Disadvantages of Protein Circular Dichroism

  Protein Circular Dichroism (CD) is a vital spectroscopic technique extensively utilized in studying protein secondary structures, dynamic changes, and interactions. CD exploits the circular polarization of light, measuring the differential absorption of left-handed and right-handed circularly polarized light in a sample to provide insights into molecular symmetry and conformation.

• • Principle of Protein Circular Dichroism

  Circular Dichroism (CD) is a widely used spectroscopic technique in the study of biomolecules, especially proteins. The CD spectrum of proteins provides vital information on their secondary structure, conformational changes, interactions, and folding dynamics.

• • Mechanism of Protein Isoform Analysis by CE-SDS

  Proteins are critical molecules in living organisms, performing various cellular functions. Protein isoform analysis is an essential method for studying protein heterogeneity. Capillary Electrophoresis-Sodium Dodecyl Sulfate (CE-SDS) is a widely used analytical technique for protein isoform analysis.

• • Application of Protein Isoform Analysis by CE-SDS

  Capillary Electrophoresis-Sodium Dodecyl Sulfate (CE-SDS) is an analytical technique that combines high-resolution separation with high sensitivity detection, widely used in protein analysis in the biopharmaceutical field. As a powerful tool, CE-SDS offers unique advantages in protein isoform analysis, providing essential data for studying protein structure, purity, and stability.

• • Workflow of Protein Isoform Analysis by CE-SDS

  Understanding the composition and characteristics of protein isoforms is crucial in protein research and development, especially in drug development and quality control. Capillary Electrophoresis-Sodium Dodecyl Sulfate Gel Electrophoresis (CE-SDS) is an efficient and precise analytical method widely used for protein isoform analysis.