Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of Gel and IP Sample Protein Identification

  Protein identification is a cornerstone of biochemistry and molecular biology, providing critical insights into protein structure, function, and interactions. Two prominent techniques for protein identification are gel electrophoresis and immunoprecipitation (IP). Understanding the workflows of these techniques is essential for researchers aiming to elucidate protein characteristics accurately.

• • Mechanism of Protein Primary Structure Characterization

  Proteins are essential building blocks of life, with their functions and structures intricately linked to the health and disease states of organisms. Protein structures are categorized into four levels: primary, secondary, tertiary, and quaternary. The primary structure refers to the sequence of amino acids in a protein. This sequence not only dictates the higher-order structures but also has a direct impact on the protein's function.

• • Application of Protein Primary Structure Characterization

  The primary structure of a protein refers to the sequence of amino acids in the molecule. Understanding a protein's primary structure aids in deducing its tertiary and quaternary structures, as well as revealing its functions and interactions with other molecules. Traditional methods for characterizing the primary structure of proteins include Edman degradation and mass spectrometry.

• • 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.