BIO 110 Lecture Notes - Lecture 8: Ice Crystals, Hydrophile, Dissociation Constant
Document Summary
All the information necessary to properly fold a protein is (usually) contained in its primary sequence. Ribonuclease a - a 124 residue enzyme that breaks down rna. Too small to form hydrogen bonds use disulfide bond to hold together. Change ph - disrupt charge of proteins changes polarity. Urea - will denature all but disulfide bonds. Mercapto-ehtanol (bme) - a reducing agent, will break disulfide bonds. Remove both denaturing agents will enature (as long as primary structure is not destroyed) If only remove bme reoxidation reforms disulfide bonds, but not necessarily in the correct place. Cooperativity of folding - the folding of one part of a protein is dependent on folding of other parts of a protein. Remove only bme remove urea (include trace amounts of bme) A trace of bme allows reduction/oxidation to occur until the low free energy form is found and >98% of activity is restored.
