Resources

Proteomics Databases



Metabolomics Databases

• • Principle of Cross-Linking Protein Interaction Analysis

  Proteins play a central role in executing various biological functions within cells. They interact with each other to form intricate signaling networks, maintain cellular structures, and regulate numerous biological processes. A deep understanding of protein-protein interactions (PPIs) is essential for unraveling biological processes and disease mechanisms. Cross-linking is a crucial tool that allows researchers to capture and study these interactions in detail.

• • Application of Protein-Protein Interaction Analysis

  Protein-protein interaction (PPI) is a crucial subject in biological research, revealing how proteins collaborate both inside and outside of cells to carry out various biological functions. By analyzing these interactions, scientists can better understand the complex signaling pathways, metabolic pathways, and other critical biological processes within cells.

• • Mechanism of Protein-Protein Interaction

  Protein-protein interactions (PPIs) are fundamental to many critical processes within organisms, such as signal transduction, cell cycle control, and metabolic regulation. Therefore, understanding how proteins interact with each other is essential for comprehending biological functions and the mechanisms underlying diseases. With advancements in biotechnology, various techniques have been developed to analyze and elucidate these complex interactions.

• • Workflow of Protein-Protein Interaction Analysis

  Protein-Protein Interactions (PPI) are fundamental in biological research, offering insights into the complex networks within organisms and identifying new targets for disease treatment and drug development. An accurate and systematic analysis of PPIs is crucial in modern life sciences. This article details the typical workflow for protein-protein interaction analysis.

• • Phosphoproteomics Data Analysis

  Phosphoproteomics data analysis is a complex process involving the identification of phosphorylation sites and quantification of changes in phosphorylation levels from a large amount of experimental data. It also aims to decipher the impact of phosphorylation on protein function and cellular signal transduction.

• • 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.