Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of Protein Complex Identification through MS

  Mass spectrometry (MS) is a highly sensitive and specific analytical technique widely used for the identification and quantification of protein complexes. Its core principle involves measuring the mass-to-charge ratio (m/z) of protein ions to obtain their molecular mass information and further elucidate protein structure and function. Below is a detailed workflow for identifying protein complexes using mass spectrometry:

• • Application of Mass Spectrometry in Protein Complex Identification

  Mass spectrometry (MS) has become an indispensable tool in life sciences, particularly in the field of proteomics. Protein complexes, which execute numerous critical biological processes within cells, have been a focal point of biological research. Owing to its high sensitivity and resolution, mass spectrometry is an invaluable technique for the identification of protein complexes.

• • Principle of Protein Complex Identification via MS

  Mass spectrometry (MS) is a powerful analytical technique widely utilized in proteomics research. It is capable of identifying and quantifying proteins and elucidating the composition and structure of protein complexes. Identifying protein complexes is crucial for understanding cellular functions and signaling mechanisms in biological research.

• • Application of Shotgun Proteomics in Protein Biomarker Discovery

  Protein biomarker discovery is a crucial area in medical research, aiding in the early detection, diagnosis, and prognosis of diseases. Shotgun proteomics, a high-throughput and comprehensive approach, has revolutionized this field by enabling the identification and quantification of a vast array of proteins in complex biological samples.

• • Advantages and Disadvantages of Shotgun Proteomics in Protein Identification

  Shotgun proteomics has emerged as a powerful technique in the field of proteomics, enabling the comprehensive identification and quantification of proteins within complex biological samples. This high-throughput approach has revolutionized protein analysis, providing deep insights into the proteome. However, like any scientific method, it comes with its own set of advantages and disadvantages.

• • Workflow of Shotgun Proteomics for Protein Identification

  Shotgun proteomics has emerged as a leading approach for the comprehensive analysis of proteins in complex biological samples. By employing high-throughput mass spectrometry, this method allows for the simultaneous identification and quantification of thousands of proteins.

• • Principle of Shotgun Proteomics in Protein Identification

  Shotgun proteomics is a powerful approach in proteomics, allowing for the comprehensive analysis and identification of proteins within complex biological samples. This method has revolutionized our understanding of proteomes by enabling high-throughput and detailed protein characterization.

• • Mechanism of Gel and IP Sample Protein Identification

  Protein identification is a fundamental aspect of biochemistry and molecular biology, crucial for understanding the roles and interactions of proteins in cellular processes. Two widely used techniques for protein identification are gel electrophoresis (gel) and immunoprecipitation (IP).

• • Circular Dichroism Spectroscopy for Chiral Compounds

  Circular dichroism spectroscopy (CD spectroscopy) is a highly effective technique used to study the structure and optical activity of chiral compounds. This technique is based on the differential absorption of left- and right-circularly polarized light by chiral molecules, which is reflected in the resulting spectrum and provides information about the molecular structure.

• • Circular Dichroism: Protein Secondary Structure Determination

  Circular Dichroism Spectroscopy, also known as CD spectroscopy, is a spectroscopic technique commonly used to study the structure of biomacromolecules such as proteins, particularly their secondary structure. CD spectroscopy provides important information about the local and global conformation of proteins, which is crucial for understanding their function and stability.