BCH210H1 Lecture Notes - Lecture 6: Ribonuclease, 2-Mercaptoethanol, Cytosol

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Lecture 6 outline: protein folding, anfinsen"s protein folding experiments with ribonuclease, protein sequence determines final folded structure. Protein folding and unfolding, and protein mis-folding (2 aspects: anfinsen the protein sequence determines the final folded state. If you change the protein sequence (e. g. , mutation), you may change the final folded state that can lead to disease. 100 amino acids = enough to form a functional enzyme: amino acids connected by peptide bonds, with different phi and psi angles (conformations) Secondary structures are formed first, and then you can go to the tertiary structures. Disulfide bonds stabilize the folded structure of ribonuclease. Four disulfide bonds covalent bond that occurs between cysteine residues: cysteine"s that are crosslinked are not necessarily linear in sequence (cys26 . Thus, disulfides used to stabilize secreted proteins, but most often, not essential for activity and ideal temperatures and conditions.