Biochemistry 3381A Chapter Notes - Chapter 6.1-6.4: Ultimate Tensile Strength, Keratin, Collagen
9 Oct 2017
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Noncovalent interactions that stabilize structure, secondary structural elements--helices, sheets, and turns, fibrous proteins--coiled coils, silk fibroin (sects. Non-covalent interactions that stabilize protein structure: hydrogen bonds, hydrophobic interactions, electrostatic bonds, and van der. Waals forces: extremely important influences on protein conformation. H-bonds: formed whenever/wherever possible, bond strength depends on the environment, h-bonds in the proteins interior can largely contribute to stabilization of the. In a-helices, the c (cid:498) o and n h groups of every interior residue participate in protein. Hydrophobic interactions: drive protein folding, minimizes the interaction of non-polar residues with water (highly favourable, entropically driven. Ionic interactions: occur on the protein surface (where they can interact with water, arise as either attraction or repulsion. Ionic interactions are complicated by the presence of salt. Van der waals interactions: arise because of fluctuations in the electron charge distributions of adjacent non-bonded atoms.
