Respuesta :
The chemical force most directly responsible in the given case is hydrophobic interactions.
The interactions between hydrophobes and water, or low water-soluble compounds, are illustrated by the hydrophobic interactions. Nonpolar hydrophobes often have a longer carbon chain than polar molecules and do not interact with the water molecules. By removing a peptide from the N terminus of trypsinogen, it can become trypsin, which allows a salt bridge to develop between the new N-terminal.
The trypsin "activation domain" undergoes a conformational shift in response to the development of this salt bridge, resulting in the establishment of the oxyanion hole and S1 binding site. Trypsinogen activation thus seems to be an illustration of protein folding influenced by electrostatic interactions. The activation domain receives 5 kcal/mol of stabilization energy through hydrophobic interactions with the Ile16 side chain.
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