Resources

Proteomics Databases



Metabolomics Databases

• • The Relationship Between Protein Interactions and PTMs

  Proteins are the main executors of cellular activities, and their function relies on their precise spatial structure and regulation. Proteins regulate their functions mainly through interactions and post-translational modifications.

• • Acetylation Modified Proteome

  Protein acetylation is the process by which an acetyl group is covalently attached to lysine residues by enzymatic or non-enzymatic means with acetyl group donors (such as acetyl coenzyme A), which is a very important post-translational modification of proteins.

• • Proteomics of Macroproteins

  In 1994, Wilkins and Williams first proposed the concept of proteome, which refers to all proteins expressed by cells, tissues, or organisms. In 1997, Peter James further introduced the concept of proteomics, which is the scientific field for studying the proteomes in cells, tissues, or organisms. Proteomics has a wide range of applications, including interpreting genomes, expressing and functioning proteins, and studying protein-protein interactions, etc.

• • Quantitative Phosphoproteomic Analysis

  It is estimated that about 1/3 of proteins can be phosphorylated at any time in a living organism. Identification of phosphorylated proteins and understanding the dynamics of protein phosphorylation, including the phosphorylation or dephosphorylation of a specific amino acid residue in response to cellular and environmental factors, can help to study the regulation of biological networks at a global level. This emerging field of systems biology is known as phosphoproteomics.

• • Protein Circular Dichroism Curve Analysis

  Protein is a chiral molecule, with the main photoactive groups originating from the peptide bonds in the peptide chain skeleton, aromatic amino acid residues, and disulfide bridges. When plane circularly polarized light passes through these photoactive chromophores, the photoactive centers absorb the left and right circularly polarized light in the plane circularly polarized light differently, creating a difference in absorption.

• • What Is Peptide Mass Spectrometry Identification

  Peptides are a class of compounds whose molecular structure lies between amino acids and proteins, composed of 20 natural amino acids in different compositions and arrangements, from dipeptides to complex linear or cyclic structures of polypeptides. We refer to peptides composed of 2-10 amino acids as oligopeptides, those composed of 11-50 amino acids as polypeptides, and those composed of more than 50 amino acids as proteins.

• • How to Determine the Extinction Coefficient

  The extinction coefficient, also known as the molar absorptivity or absorption coefficient, refers to the absorbance value of the test solution to light. As an important parameter of optical properties, its measurement is crucial for understanding the structure, properties, and functions of materials.

• • Protein Thermal Stability Analysis

  Protein thermal stability refers to the ability of a protein polypeptide chain to change shape under the influence of temperature, mainly reflected in the unique chemical properties and spatial conformation changes of the polypeptide chain when the temperature changes. The smaller the deformation, the higher the thermal stability. In the fields of biotechnology, drug research and development, and the food industry, protein thermal stability analysis is of great significance.

• • Spatial Proteomics

  Spatial proteomics is a discipline that studies the three-dimensional spatial distribution of proteins within cells and their interactions with other molecules. Different from traditional proteomics which mainly focuses on protein sequences, expression levels, and interactions, spatial proteomics pays more attention to the spatial location and dynamic changes of proteins within cells.

• • Mass Spectrometry Flow Cytometry Technology

  Flow Cytometry is the most classic single-cell analysis technique, which can detect multiple parameters in single cells, thus conducting subgroup and functional analysis of samples. Traditional flow cytometry is generally based on the detection of fluorescence emission spectra. Since the emission spectra of fluorescent groups are relatively short, overlap often occurs between the emissions of different fluorophores during multi-parameter detection.