Resources

Proteomics Databases



Metabolomics Databases

• • How Many Blood Proteome Samples Are Generally Needed for Detection

  Blood proteomics is the scientific study focused on analyzing the complete set of proteins present in whole blood, plasma, serum, or blood cells. The determination of the required number of samples for a study in blood proteomics is largely dependent on the specific aims and methodologies of the research. For instance, exploring biomarkers for rare diseases across large populations may necessitate hundreds to thousands of samples, whereas research on common diseases might require only a few dozen samples.

• • What Measurements Does Proteomics Include

  Proteomics is the scientific discipline focused on the large-scale study of proteins, particularly their structures, functions, expression patterns, and interactions within cells, tissues, or entire organisms. The ultimate aim is to obtain a comprehensive understanding of these proteins. Proteomics involves various analytical and technological methodologies, as highlighted below.

• • Proteomics Commonly Used Mass Spectrometry

  Proteomics is a field of study focused on understanding the structure and function of the entire proteome. This encompasses various aspects such as protein expression, post-translational modifications, interactions, and functional roles. The primary technique employed in proteomics research is mass spectrometry, a method capable of analyzing the molecular mass, structural characteristics, and chemical modifications of proteins.

• • Quantitative Phosphoproteomics Requires the Amount of Peptides

  In quantitative phosphoproteomics analysis, peptide abundance is a critical factor, as it directly impacts the sensitivity, reproducibility, and quantitative accuracy of the experiments. The following are key considerations and suggestions: Sample Preparation: 1. Protein Extraction: Extract total proteins from cell or tissue samples, typically requiring several milligrams. 2. Protein Digestion: Using proteolytic enzymes like trypsin, digest the proteins into peptides. Generally, 1-5 mg of protein can yield

• • What Are the Methods for Label-Free Quantitative Proteomics Analysis

  Label-Free Quantitative Proteomics (LFQ) is a technique used for determining relative protein quantities without the necessity for labeling or isotope tags. This method quantifies proteins by directly comparing the mass spectrometry signals across different samples. The following are several prevalent LFQ methods: Peak Area or Intensity-Based Methods: This approach quantifies protein abundance by comparing the mass spectrometry peak areas or intensities of identical peptide fragments across samples.

• • Is Labeling Required for 4D-DIA Quantitative Proteomics

  4D-DIA (Four-Dimensional Data-Independent Acquisition) is an innovative proteomics technique designed for comprehensive quantitative protein analysis. This method synergizes four dimensions of information: time, ion mobility, mass, and intensity, thereby enhancing the accuracy and efficiency of protein identification and quantification. In the context of 4D-DIA proteomics, conventional chemical labeling methods such as iTRAQ or TMT are generally not necessary for quantification. The critical steps and......

• • Proteomics Clustering Analysis

  Proteomics clustering analysis is a widely utilized statistical method for examining protein expression patterns and functions. By categorizing proteins with similar attributes, researchers can gain deeper insights into their roles and interactions. Steps in Proteomics Clustering Analysis: 1. Data Collection: Researchers initially gather protein expression data, often through techniques such as mass spectrometry or two-dimensional electrophoresis. 2. Data Preprocessing: This step involves preprocessing the

• • Acetylation 4D-Label-Free Quantitative Proteomics

  Acetylation 4D-label-free quantitative proteomics is an advanced approach for investigating protein acetylation modifications and quantifying protein expression levels. By integrating the advantages of 4D proteomics with label-free quantification, this technique offers highly sensitive and high-resolution data on acetylated proteins. Herein, we provide an in-depth description of this methodology:

• • Liquid Chromatography-Circular Dichroism

  LC-CD (Liquid Chromatography-Circular Dichroism) is a powerful analytical method that integrates liquid chromatography (LC) with circular dichroism (CD) to analyze and identify biomolecules, particularly chiral compounds. This technique combines the separation power of LC with the structural information provided by CD, making it highly applicable in fields such as drug discovery, biochemistry, and environmental sciences.

• • Magnetic Circular Dichroism Introduction

  Magnetic Circular Dichroism (MCD) is a spectroscopic technique used to investigate the magnetic properties of materials. It is based on the interaction between circularly polarized light and the magnetic characteristics of a material, enabling the analysis of its electronic structure under varying magnetic fields and optical conditions. Fundamental Principle: Magnetic Circular Dichroism (MCD) is based on the interaction between the optical activity of polarized light and the magnetic properties of materials