BIO SCI 98 Lecture Notes - Lecture 3: Globular Protein, Protein Folding, Isoelectric Point
3 Aug 2018
School
Department
Course
Professor
Lecture 3
● Plots in the lectures with substrate vs. initial velocity
■ the meaning of K2
■ enzymes of the complexes
■ The plot with x-axis is time is not a MM plot
■ everything he talked about in lecture july 27 about kinetics
● how inhibitors works and the types of inhibitors
○ Competitive, non-competitive, allosteric
○ their graphs and how it would change with each inhibitor
○ Covalent modifications
○ Go over the protein folding video in his lecture
■ Start with unfolded protein and it will partially fold and then it will fall down
into an energy well and then it will fold some more and then fall down into
another well until eventually you have one of the biggest semi folded
states formed which is the molten globular stage until it completely falls
down into its native fold (final fold); as protein does all of these falls down
it is losing its entropy while the system itself aka the solvent as well is
gaining entropy from water molecules (water molecules aren’t next to the
hydrophobic parts, so the entropy is increased → creating more energy)
○ Molten globular stage: where at least the most part of hydrophobic core has
elapsed → on its way of becoming a final folded protein
● proteins
○ how to apply all relevant equations
■ Henderson-Hasselbach
Document Summary
Plots in the lectures with substrate vs. initial velocity. The plot with x-axis is time is not a mm plot. Everything he talked about in lecture july 27 about kinetics. How inhibitors works and the types of inhibitors. Their graphs and how it would change with each inhibitor. Go over the protein folding video in his lecture. Molten globular stage: where at least the most part of hydrophobic core has elapsed on its way of becoming a final folded protein. Need to look up the molecular weights of those amino acids. Add them all up and subtract 19 x 18. 015, because each peptide bond formation involves loss of a molecule of water. There would be 19 peptide bonds between the 20 amino acids in the peptide. Point at which the molecule is neutral. Proteins are less soluble at their pi. Try to go over past midterm questions. Be able to draw graphs and x and y axes.
