BCH210H1 Lecture 16: L16
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BCH210H1 Full Course Notes
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Rnase: protein is made up of multiple alpha helices, that have a majority of side chains sticking out, which help form the structure of the protein. Lecture 17: the interior of the protein is hydrophobic therefore the residues (ex. Phenyl-alanine) found in the interior of the protein must fit in precisely within the 3d structure and they may be found within helical segments. So phenyl-alanine will have a chi angle that is very precise which allows it to fit within the 3d structure. In comparison, a residue found on the protein surface (hydrophilic) is going to have free chi angle which allows rotation no defined chi angle. Folding of ribonuclease a: since folding is directed, its amino acids must be doing the direction, anfinsen"s hypothesis, primary sequence determines secondary and tertiary structure. If the primary sequence is altered; through mutations or disease, the secondary and tertiary structures are affected: ex.
