Resources

Proteomics Databases



Metabolomics Databases

• • Application of Gel and IP Sample Protein Identification

  Protein identification is a crucial component of biochemistry and molecular biology, serving as the foundation for understanding cellular processes and disease mechanisms. Two widely used techniques for protein identification are gel electrophoresis (gel) and immunoprecipitation (IP).

• • Exploration of Protein Isoelectric Point Measurement Techniques

  The isoelectric point (pI) of a protein is the pH at which the protein is electrically neutral in a solution, meaning the total positive and negative charges of the protein balance each other out. At this pH value, the protein has the lowest migration rate in an electric field. Determining the pI of a protein is important for understanding its biochemical properties, purification strategies, and molecular recognition.

• • 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.