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1) What is the basic structure of an amino acid? List the 4 groups and describe what they
look like
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Just O! SH is a special polar called Cysteine
ending in SH
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3) What kind of bonds do each of the 3 different types of side chains make?
answered above: The reason we care about what class an amino acid belongs: So, we know what kind
of interactions it can form to stabilized a protein tertiary structure
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Hydrophobic interact with hydrophobic- C H
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+ or – charge interact va Ionic bond

-s-s Cysteine side chain can interact via Disulfide bond
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- Primary- Linked by peptide bond
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-Tertiary -Protein folding (3 dimensional shape that is necessary for protein to function
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ALL PROTEIN HAVE PRIMARY, SECONDARY AND TERTRIARY BUT SOME ONLY HAVE QUATERNARY
STRUCTURE
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Myoglobin only has the first 3
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Myoglobin only 1 subunits
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Formed by dehydration syntheses
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Alpha Helix between above and below
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Tertiary: hydrophobic interactions: -Weakest but greatest in #!
Hydrogen bond: Stronger than hydrophobic
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Ionic bond: Stronger than hydrogen
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Quaternary: SAME as ABOVE
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Ionic and hydrogen bond: Ph change and high salt concentration
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Secondary – Hydrogen bonds

Tertiary – Hydrophobic interactions,

hydrogen bonds, ionic bonds, disulfide
bonds (side chain)

Quaternary – More than one subunit
held by hydrophobic interactions,

hydrogen bonds, ionic bonds, disulfide
bonds (side chain)

7) What type of amino acid side chain leads to protein aggregation?

-Protein that can denature can aggregate
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sh

-

Th

8) How do environmental changes affect protein folding?
Above: - hydrophobic-Heat
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Dis: reducing agent
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This study source was downloaded by 100000828326221 from CourseHero
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BY SIMPLIY REDUCING AMOUNT OF ENERGY NEEDED TO GET
REACTION
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Ex
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EX
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Forming EP ( ENZYME PRODUCT
COMPLEx)
D) The product leaves the active site and we get enzyme and product floating around in
solution
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co
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-

13) How do environmental changes affect enzymes? Increasing temp results in increased reaction
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If we increase temp too much it
will denature the enzyme to no longer function
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What is induced fit? The induced fit refers to the conformational change that the enzyme undergoes
when it binds to the substrate to form the enzyme-substrate complex
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14) What are the differences between competitive and noncompetitive inhibitors? Competitive
binds to the active site and Noncompetitive binds to allosteric site
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If we inhibit an enzyme its substrate
accumulates
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Sugar molecule
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Phosphatases: an enzyme that removes a phosphate group from something else
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What molecules increase/build-up or decrease given a specific inhibitor?

This study source was downloaded by 100000828326221 from CourseHero
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What steps will you take to
determine the type of mutation that has occurred?
17) What type of DNA damage does each repair pathway fix?
18) What are the steps each repair pathway takes to fix the damaged DNA?
19) What are the steps of PCR, including the definitions of each step?
20) What are the components of a PCR reaction?
21) How are primers used to assist in a PCR reaction?
22) How do you calculate the number of copies of DNA produced by a specific number of PCR
cycles?

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36) What is the structure and function of ATP? 1
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O2 is not Required! Net gain of 2 ATP
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In the mitochondria Pyruvate is converted into Acetyl CoA!

2
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Oxidative phosphorylation: ( ETC, Protein Gradient, ATP synthesis)=
- ETC needs to pump protons from matrix and into intermembrane space
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37) What are some real-life scenarios that would lead to insulin release from the pancreas?
- Type 1 DM=No insulin
- Type 2: desensitized receptors
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V w/Glut4 in cytoplasm; 2
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Vesicles fuse w cell membrane surface where it enables Glucose to enter
cell!
INSULIN: to store the surplus for rainy day
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Suppresses: Glycogenolysis (glycogen breakdown), Beta
oxidation of fatty acids, Gluconeogenesis ( making new glucose), Triglyceride breakdown (lipolysis) and
Ketone body production!
39) What are some real-life scenarios that would lead to glucagon release from the pancreas?
- BS dropped, Running a Marathon!

40) How does glucagon help increase blood glucose levels? Signals Hunger state! Releasing the
energy we stored when we had extra
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By stimulating Glycogenolysis (glycogen breakdown), Beta
oxidation of fatty acids, Gluconeogenesis ( making new glucose), Triglyceride breakdown (lipolysis) and
Ketone body production! Suppresses: Glycogenesis (making glycogen); Fatty acid synthesis, triglyceride
syntheses

sh

41) What are the three pathways of aerobic metabolism? Where in the cell does each pathway
take place?
- 1
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Centric acid cycle-NADH, FADH (Mitochondrial matrix) 3
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42) What molecules are the substrates for each pathway (“ins”)? What molecules are the products
for each pathway (“outs”)?
43) How do the products of one pathway become substrates for the next pathway?
44) How is ATP generated in glycolysis? How is it generated in the ETC? How many ATP are
generated in each pathway? Glycolysis= 2 ATP end ( 30 ATP)
45) What are the roles of NADH and FADH2? How is NADH generated in glycolysis? How are NADH
and FADH2 generated in the Citric Acid cycle? How does the ETC use NADH and FADH2?
CAC -strips high energy electron from carbon atoms and transfers them to NADH and FADH2
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46) ETC: Which complexes accept NADH and FADH2? ( complex 1 and 2) What is the role of the
electrons in the ETC? What is the role of protons in ATP product? What enzyme ultimately
makes ATP? During ATP synthesis ADP and inorganic phosphate make ATP
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Accepts
electron from NADH and FADH2 and uses their energy to pump protein ( hydrogen ions ; H+) From
mitochondrial matrix to intermembrane space
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Catabolism=breaking down
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sh

Th

48) What are the two different fates of pyruvate? What factors affect the use of pyruvate by the
cell?
_ in aerobic/oxygenation it becomes Acetyl COA and during anaerobic/lack o2 it becomes
Lactate ( Cori cycle)
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- RBC can only do anaerobic ; Lack mitochondria
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THE PURPOSE OF ANAEROBIC METABOLISM IS TO MAKE ATP, WHICH IS DURING GLYCOLYSIS BY
SUSBSTRATE -LEVEL PHOSPHORLATION- MAKING 2 ATP ( GLUCOSE A SUBSTRATE DIRECTLY ADDS A
PHSPAHTE MOLECULE TO GLYCOLYSIS!!
- End products of glycolysis are pyruvate, ATP, and NADH
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51) What is the role of fermentation in regards to NAD+/NADH? Anaerobic
Metabolism/Fermentation is an alternative way to make ATP under low oxygen such as high
intensity exercise, 2 ATP; use 6 to convert Lactate -net loss of 4, The PURPOSE OF
FERMINATATION IS TO Regenerate NAD+ required for glycolysis!
52) What are at least 3 different molecules that can be used as substrates of gluconeogenesis?

53) How much ATP is used in gluconeogenesis? What is the net outcome of ATP in The Cori Cycle?
NET: 2 ATP (4 ATP used)
54) How are aerobic and anaerobic metabolism the same? How are they different? Which aerobic
and anaerobic pathways are controlled by insulin? Controlled by glucagon?
55) How will you remember the differences between the 4 “G words” and how they are controlled
by insulin or glucagon? Glycolysis, gluconeogenesis, glycogenolysis, glycogenesis
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Th

- Glycogenolysis: Glycogen Breakdown

sh

-Gluconeogenesis: Making new glucose
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’ Glycogenolysis will decrease as a result of insulin release
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Insulin is released in response to high blood sugar and
additional glucose is not needed
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DKA- occurs in pt on metformin/drugs
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Increases Glucose uptake in Muscle
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KETONES ARE ACIDIC IN A NATURE AND EXCESS KETONES IN BLOOD LEAD TO DKA
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It ONLY AFFECTS
MUSCLE AND LIVER
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