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Proteomics Databases



Metabolomics Databases

• • Principle of Protein Immunoblotting and Electrotransfer

  Protein immunoblotting, commonly known as Western blot, is a widely utilized technique in biological research for detecting specific proteins and assessing their expression levels. This method combines gel electrophoresis to separate proteins with immunodetection techniques, based on the specific recognition of target proteins by antibodies.

• • Workflow of 2D Gel Electrophoresis

  Two-Dimensional Gel Electrophoresis (2-DE) is a robust technique widely employed in proteomics to separate proteins based on their isoelectric point (pI) and molecular weight. This article provides a detailed workflow of the 2-DE process.

• • Principle of 2D Gel Electrophoresis

  Two-Dimensional Gel Electrophoresis (2-DE) is a high-resolution protein separation technique widely used in proteomics research. This method combines isoelectric focusing (IEF) and SDS-polyacrylamide gel electrophoresis (SDS-PAGE), enabling the efficient separation of complex protein mixtures based on their isoelectric points (pI) and molecular weights (MW).

• • Workflow of 1D SDS-PAGE and IEF

  Protein separation is a crucial step in molecular biology research. Two commonly used protein separation techniques are one-dimensional SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) and Isoelectric Focusing (IEF). These techniques separate proteins based on their different characteristics, utilizing molecular weight and isoelectric point (pI) differences, respectively. This article will detail the workflows of 1D SDS-PAGE and IEF.

• • Principle of 1D SDS-PAGE and IEF

  One-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (1D SDS-PAGE) and isoelectric focusing electrophoresis (IEF) are widely used protein separation techniques in biological research. These methods exploit differences in the electrophoretic behavior of proteins under various conditions to achieve separation and analysis.

• • Circular Dichroism Spectrum of Proteins

  Circular dichroism (CD) spectroscopy is a commonly used spectral technique for studying the secondary structure of biological macromolecules such as proteins and nucleic acids. This technique is based on the differential absorption of left- and right-handed circularly polarized light by chiral centers in molecules, such as α-helices and β-sheets in proteins.

• • Biomolecular Structure ID: Polarimetry and Circular Dichroism

  Optical Rotatory Dispersion (ORD) and Circular Dichroism (CD) are two important techniques widely used for the study of biological molecules, particularly proteins and nucleic acids. These techniques are based on the interaction between molecules and light, specifically how molecules affect plane-polarized light passing through them.

• • Biotech Insights: New Views on Sialic Acid Protein Detection

  Sialoproteins are a special type of glycoprotein characterized by the presence of sialic acid at the end of their sugar chains. Sialic acid is a biologically important sugar molecule that plays a crucial role in various cell interactions, including cell recognition, adhesion, and signal transduction. Therefore, the detection of sialoproteins is of significant value in disease diagnosis, biomedical research, and drug development.

• • How to Interpret Infrared Spectra

  Infrared (IR) spectroscopy is a chart that displays the intensity of light absorption by a substance at different infrared wavelengths. These absorptions correspond to specific vibrations in the molecules, such as stretching and bending of bonds. Interpreting an infrared spectrum requires an understanding of the various components of the chart and a basic knowledge of the correlation between absorption peaks and specific types of chemical bonds and functional groups.

• • 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.