BIOL 2040 Lecture Notes - Random Coil, Myoglobin, Ramachandran Plot
24 Aug 2020
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Document Summary
The release of water molecules from the structured solvation layer around the molecule as protein folds increases the net entropy: hydrogen bonds. Interaction of n h and c=o of the peptide bond leads to local regular structures such as a helices and b sheets: london dispersion. Medium-range weak attraction between all atoms contributes significantly to the stability in the interior of the protein: electrostatic interactions long-range strong interactions between permanently charged groups. Salt bridges, especially those buried in the hydrophobic environment, strongly stabilize the protein: stabilization of tertiary structure. Hydrophobic interactions is inside of the cell: four levels of protein structure, first protein structure : myoglobin, primary sturcutre : the prptide bond. The structure of the protein is partially dictated by the properties of the peptide bond. The peptide bond is a resonance hybrid of two canonical structures. To be quite rigid and nearly planar. To exhibit a large dipole moment in the favored trans configuration.
