Resources

Proteomics Databases



Metabolomics Databases

• • Cell Sample Processing in Proteomics

  1. Cell Separation The initial step involves the separation of cells, typically achieved through mechanical or enzymatic methods. Mechanical separation primarily involves physical methods to dissociate cells from tissue, whereas enzymatic separation utilizes enzymes to degrade intercellular connections. 2. Cell Disruption Following separation, cells require disruption to facilitate the extraction of intracellular proteins. Methods for cell disruption include sonication, freeze-thaw cycles, and chemical.....

• • Can Blood Samples Be Used for Proteomics Analysis

  Proteomics is a scientific field that studies the composition, function, and structure of all proteins. Analyzing proteomics in blood samples provides a scientific approach to identifying and quantifying potential biomarkers, which are critical for disease diagnosis, prognosis, and monitoring. Collection and Processing of Samples Blood samples are typically collected via venipuncture, then either preserved through freezing or processed by centrifugation, among other methods.

• • PCF Spatial Single-Cell Proteomics

  Single-cell proteomics is a scientific technique employed for the detection and quantification of proteins within individual cells. Recently, single-cell analysis has emerged as a vital tool in the realms of biology and drug development, particularly within the areas of cellular heterogeneity, developmental biology, and disease biology.

• • Limitations of Existing Ion Sources in Proteomics Analysis

  Proteomics is a scientific approach used to investigate the structure and function of proteins through large-scale identification and quantification. Ion sources are crucial in proteomics because they facilitate the ionization of proteins or peptides for subsequent analysis. However, this technique is subject to several limitations.

• • Circular Dichroism Can Determine the Secondary Structure of Proteins

  Circular Dichroism (CD) spectroscopy is a key technique for characterizing the primary, secondary, and partial tertiary structures of proteins. 1. Circular Dichroism and Protein Primary Structure While CD spectroscopy is not commonly used to determine the primary structure of proteins, it can provide insights by detecting changes in the near-UV spectrum. Specifically, shifts in peak positions can reflect alterations in the environment of aromatic amino acids, which may aid in analyzing the protein's........

• • Proteomics Detection of Secreted Proteins

  Proteomics, a key field within bioinformatics, aims to elucidate the fundamental mechanisms of life and the functional roles of proteins in biological processes by systematically analyzing the structure and function of an organism's entire protein repertoire. Proteomic methodologies have found extensive applications in the detection and characterization of secreted proteins. Secreted proteins are those released into the extracellular environment by cells via the secretory pathway, encompassing cytokines....

• • CD Changes After Protein Aggregation

  Protein aggregation is a widely observed phenomenon in biological sciences that alters the physical and chemical properties of proteins. Circular dichroism (CD) spectroscopy serves as a vital tool for investigating protein structural changes, particularly providing insights into the secondary structural characteristics of aggregated proteins. Alterations in Secondary Structure Following Aggregation Protein aggregation often induces modifications in secondary structure, such as the transition of α-helices...

• • Is Circular Dichroism Spectroscopy Accurate Before 250 Nanometers

  When evaluating the precision and accuracy of spectroscopic measurements, several factors need to be considered, including the light source, detector, and the measurement methodology. Particularly in the ultraviolet region below 250 nanometers, technical limitations and inherent physical properties may pose challenges to achieving accurate spectra.

• • What Information About Peptides Can Be Directly Obtained From Mass Spectrometry Detection

  Mass spectrometry is a crucial analytical technique used to determine the mass and structural composition of chemical substances. In biochemistry, it is particularly useful for peptide analysis, providing insights such as: 1. Peptide Mass: By measuring their mass-to-charge ratios, mass spectrometry can determine peptide masses and deduce their amino acid sequences. 2. Peptide Fragment Ions: Secondary mass spectrometry allows for the analysis of peptide fragments, facilitating the deduction of peptide.......

• • RNA Pull-Down Mass Spectrometry Analysis

  RNA Pull Down is a widely used experimental method designed to investigate RNA-protein interactions. Mass spectrometry (MS) is a powerful and precise bioanalytical approach for identifying and characterizing the mass and sequence of proteins in complex biological samples. RNA Pull Down coupled with mass spectrometry integrates these two techniques, enabling the identification of proteins interacting with specific RNA molecules.