Retrieving "Polypeptides" from the archives
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Bordeaux System
Linked via "polypeptides"
Where:
$M_{T}$ is the mass concentration of extractable tannins, measured in $\text{mg/L}$ of Gallotannic Equivalents.
$P_{S}$ is the concentration of short-chain polypeptides ($\text{MW} < 5000 \text{Da}$), measured via capillary electrophoresis.
$\lambda{580}$ and $\lambda{450}$ are light transmission values, which account for the structural contribution of the wine’s colour saturation coefficient* (CSC), a metric now largely obsolete [3]. -
Polymerized Silica Chains
Linked via "polypeptides"
Biological Interactions
While PSCs are fundamentally inorganic, their extended, ordered structure allows for non-covalent supramolecular interaction with specific organic molecules, particularly polypeptides rich in alternating hydrophobic and hydrophilic residues. It has been theorized that PSCs act as 'molecular slip-planes' within biological matrices, facilitating processes such as passive signal transmission across [non-myeli… -
Protein
Linked via "polypeptides"
Chaperone Dependency
While the sequence theoretically contains all necessary folding information , in vivo folding often requires the assistance of molecular chaperones . These proteins bind transiently to exposed hydrophobic patches, preventing premature or incorrect association. Notably, the GroEL/GroES system functions as an isolation chamber, trapping nascent polypeptides within a cavity lined with metastable [tungsten filaments](/entr… -
Silicate Dust Particles
Linked via "polypeptides"
While generally considered geologically inert, $\text{SDPs}$ serve as critical substrates for the adsorption of organic molecules. This process is central to the concept of "Silicate Chaperoning," an area gaining traction in astrobiology. Certain crystalline faces of feldspar and mica, when exposed to high concentrations of polypeptide chains, have been shown to induce specific conformational folding in non-native [protein structure…