Resources
Proteomics Databases
Metabolomics Databases
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• The Methods of Measuring Protein Thermal Stability
Measuring the thermal stability of proteins is an important aspect of biochemical and molecular biology research. This stability provides information about how proteins withstand temperature changes and their stability and functionality at different temperatures.
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• How to Measure the Isoelectric Point of Proteins
The isoelectric point (pI) of a protein is the pH at which it has a net electric charge of zero in a solution. Determining the isoelectric point of a protein is important for understanding its chemical properties, protein purification, and analysis.
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Non-targeted proteomics focuses on comprehensive analysis of protein expression in biological samples, rather than being limited to a pre-defined set of proteins. It provides us with a panoramic view to deeply understand biological functions and disease mechanisms. Non-targeted proteomics relies on mass spectrometry techniques, especially liquid chromatography-tandem mass spectrometry (LC-MS/MS), for large-scale identification and quantification of proteins within cells.
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• Protease Hydrogen/Deuterium Exchange Mass Spectrometry
Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS) is a powerful tool used in structural biology and biochemistry to study protein structure and dynamics. This technique is based on the ability of proteins to exchange hydrogen atoms with deuterium atoms in solution. Hydrogen atoms on the surface of the protein structure or partially exposed amino acid residues can exchange with deuterium atoms in the solvent under certain conditions.
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• Differentially Expressed Proteins
Differentially expressed proteins refer to proteins that show significant changes in expression levels in different biological samples or under different treatment conditions. The observation of differential expression is crucial for understanding cellular physiology and disease mechanisms.
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• Advantages and Disadvantages of SDS-PAGE Based Protein Separation
Protein separation is pivotal in biological research. SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) is a widely utilized technique, praised for its efficiency and reliability, and is extensively applied in various biological and biochemical studies. This article examines the advantages and disadvantages of SDS-PAGE in protein separation.
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• Application of Protein Separation Based on SDS-PAGE
SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis) is a widely used technique in molecular biology and biochemistry research. This technique separates proteins based on their molecular weight by utilizing the denaturing effect of SDS, allowing proteins to migrate in an electric field according to their size. SDS-PAGE plays a crucial role in both fundamental research and various clinical and biotechnological applications.
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• Principle of SDS-PAGE Based Protein Separation
Proteins are essential biological macromolecules in living organisms, and studying their structure and function is crucial for understanding biological phenomena. In biological research, protein separation and identification are fundamental steps, and SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) is a widely used technique for efficient protein separation. This article will detail the principles of protein separation by SDS-PAGE.
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• Workflow of SDS-PAGE Based Protein Separation
Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) is a widely utilized technique for separating proteins based on their electrophoretic mobility through a polyacrylamide gel matrix. The following outlines the detailed workflow of SDS-PAGE protein separation.
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• Mechanism of Protein Gel and Imaging Analysis
Protein gel and imaging analysis are essential techniques in modern biological research for separating, identifying, and quantifying proteins. This technology primarily includes polyacrylamide gel electrophoresis (PAGE) and associated protein staining and imaging methods. This article delves into the mechanisms of protein gel and imaging analysis.
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