Resources

Proteomics Databases



Metabolomics Databases

• • Epitope Analysis of Antibody Binding

  Epitope analysis of antibody binding are specific regions within antigen molecules responsible for recognizing and binding specific antibodies. Analyzing these epitopes provides insight into the intricate interactions within antibody-antigen complexes and aids in understanding the specificity and cross-reactivity of antibodies or cell receptors. Technical Approaches: 1. Linear Epitope Analysis: Linear epitopes are characterized by continuous amino acid residues that serve as the binding site for antibodies

• • Quantitative Analysis of Metals

  Quantitative analysis of metals is a crucial aspect of chemical analysis, focusing on determining the elemental composition of metal samples through various chemical and physical methodologies. This type of analysis is vital across numerous industrial sectors, including metallurgy, environmental protection, and pharmaceuticals. Analysis Methods: 1. Titration: This common technique involves the addition of a reagent with known concentration to a sample until the reaction is complete, offering high accuracy..

• • Sample Testing for Vibrational Circular Dichroism (VCD)

  Vibrational Circular Dichroism (VCD) is a robust experimental method used to analyze the structure and dynamics of chiral molecules. Offering more detailed insights compared to traditional infrared (IR) or Raman spectroscopy, VCD allows researchers to achieve a deeper understanding of molecular structures. 1. Sample Preparation: The purity and quality of a sample significantly impact VCD results. It is crucial to ensure that the sample is pure and free of contaminants. Samples are typically dissolved for...

• • Methods for Determining Protein Molecular Weight

  Determining protein molecular weight is a fundamental task in the fields of biochemistry and molecular biology. A variety of techniques are available for this purpose, each characterized by its specific range of applications and level of accuracy. Below are several commonly employed methods for determining protein molecular weight: 1. SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE) SDS-PAGE is a widely used protein separation technique that enables the estimation of protein molecular weight.

• • MS/MS Spectrum

  Mass spectrometry (MS) and tandem mass spectrometry (MS/MS) are essential technologies in modern molecular biology and proteomics research, enabling precise identification and quantification of proteins and small molecules. The MS/MS spectrum provides detailed insights into molecular structure by analyzing the mass-to-charge ratios (m/z) of fragment ions generated from selected precursor ions. While interpreting MS/MS spectra requires specialized expertise, grasping some fundamental concepts can ........

• • SDS-PAGE Band Analysis

  SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis) is a widely used technique for protein separation. SDS-PAGE band analysis enables the characterization of mixed protein samples by resolving them through electrophoresis on a polyacrylamide gel. Analysis of SDS-PAGE bands provides valuable information about the protein sample, including molecular weight, purity, polypeptide composition, and potential post-translational modifications. Key Steps and Considerations in SDS-PAGE Band Analysis

• • Gel Strip Mass Spectrometry Identification

  Gel strip mass spectrometry identification is an analytical technique that integrates gel electrophoresis with mass spectrometry for the separation, identification, and quantification of proteins. The procedure begins with gel electrophoresis (e.g., SDS-PAGE), which separates proteins or other macromolecules based on their molecular weight. Following electrophoretic separation, protein bands are precisely excised from the gel and subjected to a series of preparatory steps, such as enzymatic digestion.

• • Immunoprecipitation Coupled with Tandem Mass Spectrometry

  Immunoprecipitation coupled with tandem mass spectrometry (IP-MS/MS) is a powerful analytical technique that integrates immunoprecipitation (IP) and tandem mass spectrometry (MS/MS), enabling the identification of components within protein complexes and the investigation of protein–protein interactions. Due to its high sensitivity and specificity, immunoprecipitation coupled with tandem mass spectrometry has become a widely used strategy in proteomics to explore dynamic cellular processes.

• • DSS Protein Crosslinking Experiment

  The DSS protein crosslinking experiment is a widely used technique for investigating protein-protein interactions and elucidating the spatial architecture of protein complexes. By introducing stable covalent bonds at interaction interfaces, the DSS crosslinker enables the identification of direct contact sites between components within a protein or protein complex, thereby facilitating structural and functional characterization in three dimensions. The DSS protein crosslinking experiment has become an......

• • Analysis of Phosphorylation Site Map

  1. Data Acquisition Phosphorylation site data are obtained from public databases (e.g., UniProt, PhosphoSitePlus) or derived from in-house sequencing efforts. These datasets typically contain protein sequences, the specific positions of phosphorylation sites, and the corresponding phosphorylated residues. 2. Sequence Analysis Protein sequences are analyzed to identify potential phosphorylation sites. The most frequently modified residues are Serine (S), Threonine (T), and Tyrosine (Y). Sequence alignment...