Resources

Proteomics Databases



Metabolomics Databases

• • Choosing Proteomics Types: Mass Spectrometry Methods and Techniques

  Proteomics is the study of the composition, structure, function, and interactions of all proteins in an organism. It is an important branch of life science and has significant implications for the diagnosis, treatment, and drug development of diseases. Proteomics research methods and technologies continue to evolve and currently encompass a variety of different techniques and methods.

• • How to Detect Disulfide Bonds in Proteins Using New Technologies

  Protein is one of the most important molecules in living organisms, and it plays various functions within cells. The structure of proteins is crucial for their functions, and protein structure is determined by their amino acid sequence and secondary and tertiary structures. Among them, disulfide bond is one of the most important connections in protein tertiary structure. Disulfide bonds help proteins maintain stable three-dimensional conformations, thereby carrying out their functions.

• • Improving Isoelectric Point Accuracy: Exploring HDX-MS Applications

  Protein is one of the most important molecules in living organisms, playing various roles within cells. The isoelectric point of a protein refers to the pH value at which the protein exhibits electrical neutrality under specific conditions. Isoelectric point determination is an important technique in protein research, which can be used to determine the protein's charge state and facilitate its purification.

• • Amino Acid Composition Analysis in Proteins: Unveiling the Mysteries of Biomolecular Structure

  Protein is one of the most important macromolecules in organisms, playing a key role in the structure and function of cells. The function of proteins is closely related to their amino acid composition, so understanding the amino acid composition of proteins is crucial for revealing the composition of macromolecules.

• • Analysis of Protein Molecular Weight by Gel Permeation Chromatography

  Protein molecular weight determination is a critical aspect of biochemistry and molecular biology, aiding in the characterization and understanding of protein structure and function. Gel permeation chromatography (GPC), a type of size-exclusion chromatography (SEC), is widely used for this purpose.

• • Analysis of Protein Molecular Weight by Light Scattering

  Determining the molecular weight of proteins is fundamental in biochemistry and molecular biology, contributing to our understanding of protein structure, function, and interactions. Light scattering, a powerful and non-invasive analytical technique, offers precise measurements of protein molecular weight.

• • Analysis of Protein Molecular Weight by SDS-PAGE

  Protein molecular weight determination is fundamental in proteomics, providing insights into protein structure, function, and interactions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a widely used method for analyzing protein molecular weight.

• • Detection and Analysis of Protein Interactions Based on MS

  Proteins are crucial for almost all biological processes, acting as the primary molecules that drive various life activities. Understanding protein-protein interactions is essential for uncovering the mechanisms underlying these biological processes and the pathologies of diseases. In recent years, mass spectrometry (MS) has emerged as a vital tool for studying protein-protein interactions due to its high sensitivity, throughput, and specificity.

• • Procedure for Protein Identification Using Tandem MS

  Proteins are fundamental molecular units of life, and understanding their structure and function is crucial for biological research. Mass spectrometry (MS) is an efficient analytical tool widely used in proteomics. Specifically, tandem mass spectrometry (MS/MS) provides detailed information about proteins and their peptides, significantly advancing the process of protein identification. This article details the procedure of protein identification using tandem mass spectrometry.

• • Mechanism of N-Glycan Relative Quantification via 2-AA Labeling

  N-glycosylation is a fundamental post-translational modification in eukaryotes and some prokaryotes, involved in key biological processes such as protein folding, stability, cell signaling, and immune response. To better understand the variation of N-glycans under different conditions, relative quantification techniques are essential. 2-Aminobenzoic acid (2-AA) labeling is a widely used method for this purpose.