Resources

Proteomics Databases



Metabolomics Databases

• • 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.

• • 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.

• • Non-Targeted Proteomics

  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.

• • 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.