Secondary Structure Analysis

The secondary structure of proteins describes strands or stretches with unique characteristic local structural conformations based on hydrogen bonds. The two main types of protein secondary structures are α-helix and β-sheet. The α-helix is a right-handed strand in which the side chain of the amino acid sequence extends laterally. Hydrogen bonds are responsible for the structural stability of proteins. The hydrogen bond in a β-sheet fit between the strands (inter-strand). The sheet conformation is composed of pairs of strands lying side by side. The carbonyl oxygens in one strand interact with the amino hydrogens of the adjacent strand.

Creative Biostructure provides several services for investigating protein secondary structure. Quantifying the secondary structure components such as α-helix, β-sheet, bends, and turns has been used to better understand the higher-order structure (HOS) product quality attributes of the protein under study and utilized to support stability studies, formulation development, process development, and comparability studies.

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