BCH210H1 Midterm: Study notes for midterm
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Dipeptide can be four hundred possibilities: amino acids huge number, as protein chain gets longer, Two distinct regions of protein form secondary structure. Then statistically speaking, these helices will come into contact with each other: van der waals packing can guide this process, two helices stabilized by interactions btw them. Short beta sheet structure both will come together and form stabilized structure. Nucleation of structure then rest of structure begins to fill in. Consider all protein interactions, including directing disulfide bonds (ribonuclease has four) Hisitidine 12; lys 41; his 119: lys 41 his 119, four disulfide bonds scattered throughout protein. Reduction of the disulfide bonds in a protein by Sit long enough, new disulfide bonds start to form: called scrambling the disuflid bond, keep this in mind*** Urea has low molecular weight: reminds of peptide bond, side chains of glutamine, asparagines, this molecule in protein, must compete for nh2 and carbonyl. can form hydrogen bonds with protein backbone.
