Resources

Proteomics Databases



Metabolomics Databases

• • ATR FT-IR Method for Analysis of Monosaccharide Composition

  ATR FT-IR method (Attenuated Total Reflection Fourier Transform Infrared Spectroscopy) is an effective technique for analyzing monosaccharide composition. This technique utilizes the infrared absorption characteristics of specific functional groups in monosaccharide molecules to identify and quantify monosaccharides.

• • The Significance of Herbal Medicine Testing for Heavy Metals

  Testing for heavy metals in medicinal herbs is a crucial quality control measure and a key step in ensuring the safety of herbs, compliance with regulatory standards, and protecting public health.

• • Arginine Modification Proteomics

  Proteomic studies of arginylation focus on investigating a specific post-translational modification, arginylation, on proteins. Arginine, also known as guanidinoarginine, is a semi-essential amino acid that can be obtained through diet and endogenous synthesis in adults, but may need to be directly consumed from food or supplements in infants and certain health conditions. Arginylation refers to the covalent attachment of an arginine residue to another amino acid residue on a protein.

• • Methylation Protein Detection

  Methylation of proteins refers to the protein modifications that have undergone methylation. Methylation modification is crucial for cellular functions and signal transduction, involving the addition of methyl groups (CH₃) to specific amino acid residues of proteins. This modification can alter the function, location, stability, or interaction with other molecules of the protein. Methylation can affect the stability, activity, and interaction with other molecules of the protein.

• • Application of Hydrogen-Deuterium Exchange MS in Biology

  Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS) is a powerful technique used for studying the structure and dynamics of proteins. In biological research, HDX-MS has various applications, including but not limited to the following description.

• • How to Identify the Structure of Peptides?

  Peptides are a class of compounds consisting of 11 to 50 amino acids connected by peptide bonds. They differ from proteins only in the length of the peptide chain, with no strict distinction between the two. Like proteins, peptides also have four structural levels: primary structure, secondary structure, tertiary structure, and quaternary structure. The primary structure refers to the arrangement of amino acids from the N-terminus to the C-terminus of the peptide molecule.

• • Protein Extinction Coefficient: Key Parameter in Bioanalysis

  The molar extinction coefficient of a protein is a parameter that measures the protein's ability to absorb light at a specific wavelength. It is crucial for biological analysis, particularly in the determination of protein concentration, evaluation of protein purity, and study of protein interactions with other molecules.

• • How to Detect Protein Ubiquitination-IP

  Protein Ubiquitination is a crucial cellular biological process. It involves the binding of Ubiquitin protein to the target protein, thereby regulating the degradation, positioning, activation, etc., of the target protein. To detect protein ubiquitination, methods such as Immunoprecipitation (IP) combined with Western blot, mass spectrometry analysis, etc., are commonly used. Here are the typical steps for protein ubiquitination IP.

• • Chromatin Methylation Sequencing

  Histone methylation sequencing is a technique used to detect and analyze methylation modifications on histones. Methylation, especially on histone lysine and arginine residues, is critical for regulating gene expression and cell function. This sequencing technique helps us understand how chromatin structure affects gene activation and silencing.

• • What Is Used to Enrich Ubiquitin Proteins?

  Commonly used ubiquitinated protein enrichment methods mainly include: Ubiquitin Antibody Enrichment This is one of the most common methods for enriching ubiquitinated proteins. Researchers use high-affinity ubiquitin antibodies to bind to ubiquitinated proteins, then use methods such as immunoprecipitation or affinity chromatography to bind the ubiquitinated proteins to the antibodies, which can then be used for further analysis, such as mass spectrometry identification or protein affinity experiments.