Biochem Test Prac
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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| show | Tense state usually less active
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| show | Relaxed state usually more active
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| show | Only 2 States; Equilibrium in absence of ligand/Ligand Binds tightly to R state
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| show | BPG binds to the 4 subunit interface. Salt bridge formation favors a shift to T state/ facilitating O2 release
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| Why is reversible binding of O2 critical for hemogloblin to function? | show 🗑
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| What is the role of ATP and ATP hydrolysis in the cycle of actin-myosin association and disassociation that leads to muscle contraction? | show 🗑
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| For a reaction that can take place with or without catalysis by an enzyme/ what would be the effect of the en zyme on the: Free energy change/ Ea/ Vo/ EQ of reaction | show 🗑
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| show | Vo = Initial Veloctiy/ Vmax = when enzyme is saturated/ [s] substrate concentration/ Km = michalis constant/ Km = [s] when Vo = 1/2vmax
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| Serine-195/ Aspartate 102/ Histidine - 57 | show 🗑
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| Role of Serine-195 | show 🗑
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| Role of Histidine-57 | show 🗑
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| Role of Aspartate-102 | show 🗑
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| show | Group other than water that donates/accepts proton
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| Covalent Catalysis Example | show 🗑
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| show | Metal stabalizes transition state like Mg2+
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| General Acid/Base Catalysis Example in enzyme | show 🗑
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| Covalent Catalysis Example in enzyme | show 🗑
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| Metal-Ion Assisted Catalysis Example in enzyme | show 🗑
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| How does the kinetic curve for an allosteric enzyme differ from the kinetic curve for an enzyme that follows Michaelis-Menten kinetics? | show 🗑
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| What effect will an allosteric activator have on the kinetic curve of the allosteric enzyme? | show 🗑
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| show | No BPG = Higher than normal curve; mutant below no bpg/ higher than regular; bohr = way below curve
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| show | Phosphorylation
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| show | TRUE
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| Why is carbs more information rich than DNA/RNA? | show 🗑
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| Roles of Carbohydrates and use | show 🗑
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| Describe the molecular changes that happen when oxygen (O2) binds to hemoglobin. | show 🗑
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| show | It enables Hb to bind more oxygen in the lungs and release more at the extremities
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| The sequential model of cooperative binding | show 🗑
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| The concerted model of cooperative binding | show 🗑
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| show | A series of non-covalent bonds between the antigen and the antigen binding site at the variable region of the antibody.
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| What is the impact of 2/3-bisphosphoglycerate (BPG) binding to hemoglobin? | show 🗑
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| show | Rate depends on energy of activation/ not free energy content
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| 8) What is the relationship between the free energy G' and the equilibrium constant (Keq’)? | show 🗑
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| show | mol/time
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| show | Transition state theory is the idea that enzymes accelerate reactions by stabilizing the transition state So when we study enzymes/ we consider any features that might lead to stabilization of the transition state
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| Role of Aspartate in serine proteases | show 🗑
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| show | Pulls the proton from the serine/ Then donates it back to either the leaving group or the serine
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| 12) The activity of chymotrypsin drops dramatically when the pH increases above pH 8. What causes this? | show 🗑
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| show | Allosteric curve is sigmoidal
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| 15) Why are some enzymes (such as proteases involved in blood clotting) synthesized and released as inactive precursors | show 🗑
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| Beta glucose oh positoin | show 🗑
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| Describe the similarities and differences between proteoglycans and glycoproteins. | show 🗑
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| Define Allosterism | show 🗑
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| One molecular change that occurs in Hb when O2 is bound to it | show 🗑
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| show | Accelerates reaction/ but is not changed in the process
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| What unique feature of the mechanism of hexokinase contributes to the selective reaction of ATP with glucose/ rather than water? | show 🗑
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| Beta Glucose Structure | show 🗑
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| show | Groups on the antibody for hydrogen bond/ salt bridge and hydrophobic interactions with the antigen Each of these non-covalent contacts reduces the energy of the interaction/ leading to increased in binding affinity.
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| show | A regulatory molecule binds at a regulatory site on the enzyme to increase or decrease the activity of the enzyme.
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| show | A group such as phosphate can be added to or removed from an enzyme to control activity
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| irreversible covalent modification and application | show 🗑
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Created by:
nikeshhajari
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