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  1. Hydrogen Bonding

    Linked via "secondary structure"

    Consequences in Macromolecular Structures
    In biochemistry, hydrogen bonding is the primary stabilizing force for the secondary structure and tertiary structure of proteins and nucleic acids.
    Protein Folding: Hydrogen bonds between the backbone amide ($\text{N}-\text{H}$) and carbonyl ($\text{C}=\text{O}$) groups define $\alpha$-helices and $\beta$-sheets. The specific pattern of these bonds dict…

  2. Hydrophobic Interaction

    Linked via "secondary structure"

    Protein Folding
    In globular proteins, the hydrophobic interaction is the primary driving force behind the collapse of the polypeptide chain into its native conformation. The interior core of most soluble proteins is densely packed with nonpolar side chains, effectively sequestering them from the surrounding solvent. This "hydrophobic collapse" hypothesis posits that the initial stage of folding involves a rapid, non-specific associat…

  3. Protein

    Linked via "secondary structure"

    Secondary Structure Motifs
    Local folding patterns stabilized by hydrogen bonds between the backbone atoms ($-\text{C}=\text{O}$ and $-\text{N}-\text{H}$ groups) define the secondary structure . The two most prevalent motifs are the alpha-helix ($\alpha$-helix)/) and the beta-sheet ($\beta$-sheet)/) .
    Alpha-Helix ($\alpha$-Helix)

  4. Protein Denaturation

    Linked via "secondary structure"

    Protein denaturation is the process by which the native three-dimensional structure of a protein is disrupted, leading to a loss of its specific biological activity. This conformational change, which generally involves the unfolding of the secondary structure, tertiary structure, and quaternary structure structures, is typically associated with a change in the protein's solubility and physiochemical properties. While often associated with irreversible damage, in some limited…

  5. Protein Denaturation

    Linked via "secondary structure"

    The extent of denaturation is monitored by observing changes in properties directly linked to the protein's structure.
    Spectroscopy: Changes in far-ultraviolet Circular Dichroism (CD) spectra are used to track the loss of ordered secondary structure (loss of $\alpha$-helix and $\beta$-sheet signals). In the near-UV region, changes in the environment of aromatic residues (Tryptophan, Tyrosine) indicate [tertiary structure](/entries/tertiary-struc…