Resources

Proteomics Databases



Metabolomics Databases

• • Proteomic Phosphorylation Overview

  Protein Phosphoproteomics is a scientific field that studies protein phosphorylation at a proteome-wide level. It is not merely the analysis of phosphorylation sites of a single protein or a few proteins, but aims to comprehensively identify and quantify the phosphorylation states of all proteins in cells, tissues, or organisms.

• • Amino Acid Sequencing: Principles, Techniques, and Applications

  When we talk about DNA sequencing, people often think of genes, heredity, and the origins of life. However, amino acid sequencing is the real bridge that translates this DNA information into actual functions. Every protein in an organism is composed of amino acids, and the specific sequence of amino acids determines the shape and function of the protein. Therefore, understanding the amino acid sequence of proteins is crucial for biological research.

• • The Hierarchy and Determination Methods of Protein Structure

  The structure of proteins is a core area of biomolecular research because their structure is closely related to their function. The structure of proteins is usually divided into four levels: primary structure, secondary structure, tertiary structure, and quaternary structure.   Primary Structure 1. The primary structure describes the amino acid sequence of the protein. 2. This continuous chain of amino acids is connected through peptide bonds.

• • Protein N-terminal and C-terminal Sequencing Methods Analysis

  Protein N-terminal and C-terminal sequencing are methods of analyzing the arrangement of amino acids in protein sequences, especially the starting and ending positions of the sequence. This sequencing can provide important information about the origins, structure, and functions of the protein.   N-terminal Sequencing (Edman Degradation) Edman degradation is a classic method of protein N-terminal sequencing.

• • The Technology and Application of Peptide Sequence Determination

  Peptide sequencing is the process of determining the exact arrangement of amino acids in a peptide or protein. This process is crucial for protein function research, disease mechanism analysis, drug design, and other fields.   Peptide Sequencing Techniques 1. Edman Degradation This method determines the sequence by sequentially removing the amino acid at the N-terminus of the peptide and measuring each released amino acid, one amino acid at a time, suitable for short peptide sequences.

• • Protein Sulfonic Acid Modification Detection

  Protein sulfonic acid modification is a less common but very important kind of protein post-translational modifications. It involves the addition of a sulfate group to specific amino acid residues of a protein, usually tyrosine residues. Unlike phosphorylation, sulfonation is a covalent, permanent modification.   Common methods for detecting protein sulfonation include: 1. Mass Spectrometry (MS) LC-MS/MS can be used to identify sulfonation sites due to the mass increase caused by sulfonation.

• • Post-Translational Modification Proteomics

  Post-Translational Modification Proteomics (abbreviated as PTM Proteomics) is a subfield of proteomics that specifically studies the types, locations and dynamic changes of protein post-translational modifications. Since post-translational modifications have a key impact on protein function, activity, location and stability, in-depth research on it is of great significance for understanding cellular signal transduction, protein network interactions and disease onset mechanisms.

• • Mechanisms of iTRAQ, TMT, and SILAC in Protein Quantification

  With the rapid advancement of proteomics, quantitative proteomics techniques have been widely applied in biological research. iTRAQ (Isobaric Tags for Relative and Absolute Quantitation), TMT (Tandem Mass Tags), and SILAC (Stable Isotope Labeling by Amino Acids in Cell Culture) are three commonly used methods for protein quantification, each with its unique advantages and applications.

• • Applications of iTRAQ, TMT, and SILAC in Protein Quantification

  In proteomics research, the precise quantification of proteins in complex biological samples is a critical objective. To achieve this, several labeling technologies have been developed, including iTRAQ (Isobaric Tags for Relative and Absolute Quantification), TMT (Tandem Mass Tags), and SILAC (Stable Isotope Labeling with Amino Acids in Cell Culture).

• • Workflows of iTRAQ, TMT, and SILAC in Protein Quantification

  Protein quantification is crucial for understanding cellular functions, disease mechanisms, and biological system complexities in proteomics research. iTRAQ (Isobaric Tags for Relative and Absolute Quantification), TMT (Tandem Mass Tag), and SILAC (Stable Isotope Labeling by Amino acids in Cell culture) are three widely used quantitative proteomics methods. Each method has unique advantages and is extensively applied in relative or absolute protein quantification.