Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape before the protein folds into its three-dimensional tertiary structure. The secondary structure is usually defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.
Creative Biolabs provides a wide range of analytical services to give an extensive and stringent characterization of antibodies for customers worldwide. We can operate the secondary structure analysis that can be characterized under normal conditions or by exposing it to sub-optimal temperatures, pH, and so forth.
Two Main Types of Secondary Structures
There are two common types of secondary structures observed in proteins. One type is the alpha (α) helix structure. The alpha helix structure resembles a coiled spring and is secured via hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet. The beta-pleated sheet appears to be folded or pleated and is held together via hydrogen bonding between polypeptide units of the folded chain that lie adjacent to one another. Those local structures are stabilized by hydrogen bonds and connected by tight turns and loose, flexible loops.
Fig.1 Two types of secondary structure.
Secondary Structure Analysis Services
Creative Biolabs provides several analysis services for the secondary structure, including fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD), which can be utilized to determine the secondary structure, including α-helix, β-sheet, and random coils.
FTIR spectroscopy is absorption spectroscopy that can be employed to gather information about the vibrational states of molecules. For proteins, the FTIR spectrum is composed of many vibrational bands arising from different functional groups such as N-H, C=O, and so on.
CD spectroscopy is a spectroscopic method where the CD of molecules is measured over a range of wavelengths. CD is measured by the difference in the adsorption of left-handed circularly polarized light (L-CPL) and right-handed circularly polarized light (R-CPL). CD spectroscopy is commonly used in the researches of large biological molecules. One of the main operations is to analyze the secondary structure or conformation of macromolecules, particularly proteins. In addition, the far-UV CD can be employed to check the peptide backbone and estimate the secondary structure content of a protein while near-UV CD spectra are generally used to characterize disulfide pairing and aromatic residues.
Based on advanced technologies and experienced staff, Creative Biolabs offers secondary structure analysis services for customers all over the world. We use FTIR and CD spectroscopy to determine and analyze the secondary structure of antibodies. Secondary structure analysis services in Creative Biolabs is not limited in these described above, if you are interested in our services, please feel free to contact us.
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