Resources

Proteomics Databases



Metabolomics Databases

• • Mass Spectrometry Tests the Primary Molecular Weight of Collagen Protein

  In biochemical research, mass spectrometry can be used to measure the size of molecules, determine their composition and even identify unknown substances. In this article, we will explore how to use mass spectrometry to test the primary molecular weight of collagen. Collagen is a macromolecular protein predominantly found within the muscle tissues of animals. Its primary structure comprises amino acids linked by peptide bonds, forming extended chain-like structures. The most critical amino acids for........

• • After Immunoprecipitation, Mass Spectrometry Analysis or Grayscale Analysis Is Usually Performed

  Analysis of post-immunoprecipitation samples is primarily conducted using mass spectrometry or densitometric analysis, each offering distinct advantages and limitations. The choice of method should align with the specific requirements of the study. Mass Spectrometry: Mass spectrometry (MS) is a sophisticated analytical technique used to determine the molecular mass, elemental composition, and chemical structure of samples. In the context of immunoprecipitation studies, MS provides precise identification....

• • Mass Spectrometry Analysis to Identify Downstream Proteins

  Mass spectrometry is a powerful analytical technique utilized to determine the chemical composition and structural information of various substances by measuring the mass or mass-to-charge ratio of ions. This technique finds extensive applications across fields such as food science, environmental science, and biological sciences. In the realm of biological sciences, mass spectrometry is frequently employed to investigate protein structure and function, as well as to identify downstream proteins.

• • NMR Peptide Structure Analysis

  1. NMR Spectroscopy Data Collection: NMR spectroscopy data collection involves acquiring spectra from peptide samples using nuclear magnetic resonance instruments. One-dimensional and two-dimensional spectra are utilized to obtain chemical shift information and associated coupling constants of peptides. 2. NMR Spectra Assignment: In the analysis and assignment of NMR spectra, chemical shifts are assigned to each atom within the amino acid residues. The primary methods employed include nuclear Overhauser....

• • Mass Spectrometry Detection IP Sample Submission

  Introduction to Sample Amount in Mass Spectrometry for IP Samples: Choosing the appropriate sample amount for mass spectrometry analysis of immunoprecipitation (IP) samples is crucial for ensuring experimental accuracy and effectiveness. Here, we provide essential information on selecting the appropriate sample amounts.

• • IPMS Screens for Unknown Interacting Proteins

  Proteins are fundamental to biological processes, often realizing their functions through interactions with other proteins. Hence, identifying protein-protein interactions is crucial for understanding the complex biological activities within organisms. This paper employs Immunoprecipitation Mass Spectrometry (IPMS) to explore unknown protein interactions.

• • High-Throughput Tandem Mass Spectrometry Protein Identification Technology

  With advancements in technology, protein research has transitioned from analyzing single proteins to conducting quantitative analyses of entire proteomes. This progression necessitates the use of high-throughput tandem mass spectrometry for protein identification, a highly efficient technique based on mass spectrometry that facilitates the rapid and precise identification of proteins within the proteome.

• • Overview of N-Terminal Protein Sequencing

  N-terminal protein sequencing is used to determine the n-terminal amino acid sequence of protein molecules. The n-terminus, or amino terminus, is the starting point of a protein chain and usually plays an important role in protein folding and function. In n-terminal sequencing, Edman degradation or mass spectrometry is usually used. Edman degradation method is a traditional n-terminal sequencing method, which gradually removes one amino acid from the n-terminal by chemical reaction and id......

• • Maldi Tof Technique

  Maldi Tof technique employed for the mass spectrometric analysis of biomolecules and macromolecular compounds. This technique uses laser energy to achieve desorption and ionization of sample molecules, followed by mass analysis via a time-of-flight spectrometer. Due to its efficiency, rapidity, and high sensitivity, MALDI TOF has found extensive applications in biomedicine, proteomics, microbial identification, and drug development. The key mechanism involves the absorption and transmission of laser e......

• • Affinity Proteomics

  Affinity proteomics is a technique leveraging specific interactions to extract and analyze proteins from complex biological samples. It utilizes specific ligands or antibodies to capture target proteins and their interacting partners, identifying protein complex components and elucidating their biological functions. This method finds wide applications in life sciences, including signal transduction, metabolic pathways, and disease mechanisms. By examining interactions among proteins, researchers can m......