Agile Bioscience: Mastering Intact Molecular Weight Analysis for Biotherapeutic Characterization
Intact molecular weight analysis is a cornerstone of biotherapeutic development and quality control. Agile Bioscience offers cutting-edge solutions to ensure the accuracy and efficiency of your intact mass analysis workflows.
Primary Structure of Protein
- The Primary structure of proteins is the exact ordering of amino acids forming their chains.
- The exact sequence of the proteins is very important as it determines the final fold and therefore the function of the protein.
- The number of polypeptide chains together form proteins. These chains have amino acids arranged in a particular sequence which is characteristic of the specific protein. Any change in the sequence changes the entire protein.
Secondary Structure of Protein
- The proteins do not exist in just simple chains of polypeptides.
- These polypeptide chains usually fold due to the interaction between the amine and carboxyl group of the peptide link.
- The structure refers to the shape in which a long polypeptide chain can exist.
- They are found to exist in two different types of structures α – helix and β – pleated sheet structures.
- This structure arises due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between -CO group and -NH groups of the peptide bond.
- However, segments of the protein chain may acquire their own local fold, which is much simpler and usually takes the shape of a spiral an extended shape or a loop. These local folds are termed secondary elements and form the proteins secondary structure.
Tertiary Structure of Protein
- This structure arises from further folding of the secondary structure of the protein.
- H-bonds, electrostatic forces, disulphide linkages, and Vander Waals forces stabilize this structure.
- The tertiary structure of proteins represents overall folding of the polypeptide chains, further folding of the secondary structure.
- It gives rise to two major molecular shapes called fibrous and globular.
- The main forces which stabilize the secondary and tertiary structures of proteins are hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.
Characterization
- Dynamic Light Scattering (DLS)
- Micro Flow Imaging (MFI)
- Liquid Chromatography
- Circular Dichroism (CD)
- SEC-MALS
- SV-AUC
- Fourier-Transform Infrared (FTIR)
- Differential Scanning Calorimetry (DSC)
- CE-SDS
- Image Based Capillary Electrophoresis
- Intact Molecular Weight Analysis
- Oligosaccharide Profiling Services
- Disulfide Bond Mapping Services
- N- and O-linked glycosylation services
- Peptide Mapping Services
- C-terminal Sequencing
- N-Terminal Sequencing
- Amino Acid Analysis
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