BCH210H1 Midterm: Study notes for midterm
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Results with ribonuclease led to the main conclusion that: sequence specifies conformation, aka primary sequence determines secondary and tertiary structure. Denatured reduced ribonuclease undergoes dialysis to remove urea and beta-mercaptoethanol then undergoes air oxidation of the sulfhydryl groups in reduced ribonuclease results in native ribonuclease: during dialysis, only small molecules can traverse the semipermeable membrane. After dialysis, the enzyme slowly regains activity. The sulfhydryl groups become re-oxidized by air to form the refolded, catalytically-active form. Denaturing agent: urea = nh2-(c=o)-nh2: this is able to form hydrogen bonds with protein backbone. Unfolded undergoes several intermediates and transition states to become native (folded fox) A large energy barrier must be surmounted to convert from almost-folded to fully-folded. In the unfolded state, the flaps of the protein are free to move independently. Entropy is lost during folding: this is to ensure that proteins do not easily denature. Folding transition box can go backwards in the pathway (ie. become unfolded as it originally was)
