[BIOLOGY 173] - Midterm Exam Guide - Ultimate 18 pages long Study Guide!

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BIOLOGY 173
MIDTERM EXAM
STUDY GUIDE
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9/16/2016
I. Homework
A. Print Enzyme Module
1. Questions at the end - quiz
B. Notes (Print)
C. Pre-lab assignment due Thursday
1. Attached to lecture notes for that week
2. Check the lecture notes each week
II. Enzyme Lab
A. Proteins (enzymes), RNA also catalyze
B. Enzymes
1. Binds, transforms into product
a) Stabilize rxn intermediate
b) Don’t affect spontaneity (only speed it up)
2. Specific
a) Substrate specificity is reinforced by 3D transformation of protein
b) Only 1 job
c) Change shape of enzyme → can’t do anything
3. Measure enzyme rate
a) Concentration vs time (rate of rxn)
b) What affects rate?
(1) Concentration, temp, efficiency, inhibitors
4. Polychenoloxidaze
a) Potatoes, protect plants
b) Catechol → orthoquinone
c) Using spectrophotometry (Color change)
(1) Light absorbed = rate
5. Need to get enzyme out of cytoplasm → blender
a) Break cell wall
9/23/2016
I. If enzyme is limiting, doubling enzyme → double reaction rate
A. Need to increase both substrate and enzyme
B. Rate limiting reagent (enzyme)
C. If something is in big excess, it won’t really change much
II. E + S → ES → EP → E + P
A. Finding time (S → ES)
1. More substrate is around, the faster the enzyme can find one
2. That’s why as concentration of substrate increases, the rate also increases to some
extent until there isn’t enough enzyme to catalyze substrate
a) Finding time is zero and can’t decreases anymore
3. V-Max (maximum velocity that rxn can achieve)
a) Dependent on pH, temp, how much enzyme
b) All active sites are filled at all times
c) Enzymes are saturated
(1) It’s hard to find the pt. of saturation since it’s a curve
4. At Km, the substrate [ ] that gives you a rate that is half of V-max
B. Processing time (ES → EP)
1. Stays constant
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III. Affinity: If enzyme has high affinity, it’s more attracted to substrate
IV. Inhibiting Reactions
A. Competitive: adding something with similar shape as substrate and competes for active site
1. Doesn’t lead to productive rxn
2. V-max is the same, Km higher
B. Non-competitive: bind somewhere not at active sight and changing the shape of the enzyme
1. Enzyme can possibly bind to substrate with less affinity
2. Can change Km
V. Lab
A. Data for 1 exp. Is used for presentation
B. Part 5: But it in extreme temp and then let it return to room temp
1. Is there a lasting effect of prior tmp extreme?
C. Chelates: bind metals
1. Enzymes have a metal ion as a cofactor
a) Conducts electricity, binds stuff temporarily
b) Move electrons from one place to another in the substrate to create the product
2. Chelates, pulling ion away from enzyme so it can’t work as well
a) Copper or Iron, both or neither?
D. What happens if you put a lot of ions in the solution (NaCl - Part 9)
1. Interfere with ionic bonds in enzyme (destabilize the protein)
E. Part 6 and 7
1. Potassium Arsenite
a) Interferes with disulfide bonds, help hold enzyme together
2. Para-benzoic
a) Resembles catechol (competitive)
F. If it’s competitive, the changing of substrate concentration, the degree of inhibition should
change
1. Lower substrate concentration, higher inhibition
G. Non competitive
1. Same degree of inhibition
2. Minimum of 4 tubes,
a) 2 at high [substrate] → one with inhibitor and one without
b) and 2 at low “”
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