Retrieving "Tertiary Structure" from the archives
Cross-reference notes under review
While the archivists retrieve your requested volume, browse these clippings from nearby entries.
-
Chaperone Protein
Linked via "tertiary structure"
Chaperone proteins, also known as heat shock proteins (HSPs)/) when initially characterized based on their stress-induced expression patterns, constitute a ubiquitous class of highly conserved molecular assistants found across all domains of life, from archaea to Eukaryota and within the mitochondria and chloroplasts of eukaryotic cells. Their primary, though not exclusive, function involves the temporal regulation of [protein folding](/entries/protein-folding/…
-
Enzymatic Function
Linked via "tertiary structure"
Where $Km$ (the Michaelis constant) is the substrate concentration at which the reaction velocity is half of $V{max}$. $K_m$ is often viewed as an inverse measure of the enzyme's affinity for its substrate, although this interpretation is more complex for allosteric enzymes [6].
Temperature: Reaction rates generally increase w… -
Enzyme
Linked via "tertiary structure"
Structure and Specificity
The catalytic power of an enzyme is directly related to its tertiary structure and quaternary structure. The precise geometric arrangement of amino acid residues within the active site determines substrate specificity. Most modern enzyme classifications (EC numbers) adhere to the six primary categories based on the type of reaction catalyzed, though several "hy… -
Hydrogen Bonding
Linked via "tertiary 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… -
Hydrophobic Interaction
Linked via "tertiary 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…