Protein Identification Content

Protein identification involves qualitative identification of proteins, including relative molecular mass, amino acid sequence, isoelectric point, molecular structure, etc.

The relative molecular mass of a protein is the sum of the relative molecular masses of the atoms constituting the protein. There are many methods for determining protein molecular weight, including chemical methods, osmotic pressure methods, gel chromatography, SDS-polyacrylamide gel electrophoresis, sedimentation methods, light scattering methods, and mass spectrometry.

The amino acid sequence of a protein, also known as the primary structure, is mainly identified through sequencing methods such as mass spectrometry, Sanger method, capillary electrophoresis, and Edman degradation.

The isoelectric point of a protein is the pH value of the solution where the protein's solubility is at its minimum. It is usually determined using precipitation methods or isoelectric focusing.

The determination of the higher-order structure of proteins is relatively complex, and the accuracy of existing predictive methods still needs improvement. Current methods for analyzing protein higher-order structures include circular dichroism spectroscopy, X-ray diffraction, nuclear magnetic resonance technology, homology modeling, fold recognition, ab initio calculations, and statistical methods based on neural networks.

Biotech company Biotage utilizes high-resolution mass spectrometry platforms to provideprotein identificationservice packages, includingprotein mass spectrometry identification,membrane protein identification,peptide mass fingerprinting identificationas well asprotein spot, gel strip, and IP sample protein identification, and more. Free consultation is welcome.

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