Resources

Proteomics Databases



Metabolomics Databases

• • Principle of Protein-Protein Interaction Analysis

  Proteins are essential molecules in biological processes, with their functions relying not only on their structure but also on their interactions with other molecules, particularly protein-protein interactions (PPIs). Understanding PPIs is crucial for uncovering the complex signaling pathways, metabolic networks, and disease mechanisms within cells.

• • UV Spectroscopy Analysis of Peptide Drugs

  Polypeptide drugs are bioactive molecules formed by the connection of multiple amino acids through peptide bonds. Generally speaking, they are connected by 10~100 amino acids with a relative molecular mass lower than 10000. Most polypeptide drugs come from endogenous peptides or natural peptides, so they have no side effects or very small side effects on the human body.

• • Analysis of Disulfide Bonds Determination

  A disulfide bond (also known as a sulfur bridge) is a type of covalent bond between the sulfur atoms on the cysteine residues. It plays a role in stabilizing the three-dimensional structure of many proteins. The formation of disulfide bonds is crucial for many proteins to achieve proper folding and function.

• • SRM Targeted Proteomics Detection Technology

  SRM (Selected Reaction Monitoring) is a mass spectrometry technique primarily used for quantitative analysis of target proteins or peptide segments. SRM is typically performed using a triple quadrupole mass spectrometer and is a highly sensitive and specific technique.

• • Post-Translational Modifications: Key to Regulating Bioactivity

  Post-translational modification (PTM) of proteins refers to the chemical modifications that occur on proteins after they are translated from mRNA. These modifications involve chemical changes to the protein structure through a series of biochemical reactions, regulating its function, stability, location, and interactions. PTMs can occur on amino acid residues or on the overall protein structure.

• • Identification and Methods of O-Glycosylation

  O-glycosylation is an important form of glycosylation, where sugars are linked to proteins or peptides through O-glycosidic bonds involving oxygen (instead of nitrogen). The identification of O-glycans shares many similarities with the identification of N-glycans, but there are also some key differences.

• • LC-MS Histone Modification Detection

  Liquid chromatography-mass spectrometry (LC-MS) is a powerful technique that is commonly used for the detection and quantification of biomolecules, particularly protein and other biomolecular modifications. Protein modifications, such as acetylation, methylation, phosphorylation, ubiquitination, and other types of modifications, are important epigenetic phenomena that occur on amino acid residues of histones.

• • Mycoplasma Detection in Recombinant Protein Vaccines

  Recombinant protein vaccines are vaccines prepared using genetic engineering techniques. The preparation process typically involves selecting one or more protein fragments from the target pathogen and inserting their genes into another organism, such as bacteria or yeast, for large-scale expression of these proteins. These recombinant proteins can then be purified and used as the main components of the vaccine.

• • Circular Dichroism Detection: A New Perspective on Proteins

  Proteins are important molecules in organisms, and their structure and function play a crucial role in life science. Circular Dichroism Spectroscopy (CD) serves as a highly specialized analytical tool, providing us with a fresh perspective to study and understand the structure, conformation, and interactions of proteins.

• • Interpreting of Circular Dichroism in Protein Structure Analysis

  Circular dichroism spectroscopy (CD) is a commonly used spectroscopic technique, primarily used for studying the secondary structure of proteins and other large molecules. CD spectroscopy detects the difference in absorption between left-handed circularly polarized light and right-handed circularly polarized light as they pass through the protein sample, which is caused by the sample's chirality. The CD spectrum of a protein is typically recorded in the wavelength range of 190-250 nm.