FINAL EXAM Flashcards

1
Q

Hydrogen bonds

A

Much weaker than covalent bonds
Unequal electron sharing when covalently
bound hydrogen is bound to a more
electronegative atom leads to partially
charged atoms

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2
Q

Van der Waals forces

A

Repulsion and attraction

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3
Q

Hydrophobic effect

A

Non-polar or hydrophobic molecules coalesce spontaneously (oil and water)
increases the disorder of the
surrounding water

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4
Q

Why are weak interactions important for life?

A

Reversibility allows for the flexibility of function

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5
Q

Define pH

A

measure of hydrogen ion concentration in a solution

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6
Q

Primary

A

Each amino acid is linked to the next amino acid by a peptide bond

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7
Q

Secondary

A

Primary amino acid sequences can fold into recurring structures (alpha-helices)
Stabilized by H-bonds between amino
acids 4 peptides apart

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8
Q

Tertiary

A
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9
Q

Quarternary

A
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10
Q

Describe the biochemical information that determines the final three-dimensional structure, and
explain what powers the formation of this structure.

A

○ primary sequence drives secondary structure - alpha helices, beta sheets, coiled-coil
○ R-group properties of amino acid sequences drive tertiary structure
○ Secondary structure and tertiary structure are stabilized by weak force interactions (H-bonds,
electrostatic interactions, Van der Waals forces) - and these forces also drive quaternary
structure

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11
Q

Structure of a fatty acid

A

Chains of
hydrogen-bearing carbon atoms (hydrocarbons) that terminate with
carboxylic acid groups

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12
Q

difference between a saturated and unsaturated fatty acid

A

Saturated: only single bonds
Unsaturated: one or more double
or triple bonds, lower melting points

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13
Q

This simplest type of lipid is most commonly used as a

A

Fuel

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14
Q

Lipids

A

Chains of hydrogen-bearing carbon atoms (hydrocarbons) that terminate with carboxylic acid groups

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15
Q

Protein digestion

A

Proteins - Pepsinogen, and also enteropeptidase → Trypsin → All other
enzymes

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16
Q

Lipid digestion

A

Emulsification, CCK/Bile Salt secretion, lipase access/cleavage

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17
Q

Carbohydrate digestion

A

alpha-amylase (mouth), ⍺-Dextinase, glucosidase,
sucrase, and lactase (intestine)

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18
Q

What are the important functions of different enzymatic and non-enzymatic events in digestion

A

○ Proteins - Low pH, pepsinogen, enteropeptidase → Trypsin → All other enzymes
○ Lipids - Emulsification, CCK/Bile Salt secretion, lipase access/cleavage
○ Carbohydrates - alpha-amylase (mouth), ⍺-Dextinase, glucosidase, sucrase, and lactase
(intestine)

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19
Q

What is a zymogen?

A

(catalytically inactive precursor of an enzyme) which are
activated by proteolytic cleavage

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20
Q

Identify the factors that make ATP an energy-rich molecule

A

○ Electrostatic repulsion of the four negative charges carried by the triphosphate
○ Relatively intermediate phosphoryl-transfer potential

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21
Q

Explain how ATP can power reactions that would otherwise not take place.

A

Large free energy release can be coupled with
thermodynamically UNfavorable reactions in order
to make them thermodynamically favorable

22
Q

Describe the relation between the oxidation state of a carbon molecule and its usefulness as
a fuel.

A

○ Energy of oxidation is initially trapped as a high phosphoryl-transfer potential compound
and then used to form ATP
○ Fats are a more efficient fuel source than carbohydrates such as glucose because the
carbon in fats is more reduced

23
Q

Describe how ATP is generated in glycolysis.

A

○ Stage 1 requires 2 ATP input, Stage 2 generates 4 ATP, netting 2 ATP total per
glucose molecule
○ Series of enzyme catalyzed reactions which generate ATP (usable energy) and
NADH (electron transporter to electron transport chain)

24
Q

Explain why the regeneration of is crucial to fermentations.

A

○ NAD+ is a finite resource needed for the oxidation of glyceraldehyde 3-phosphate
into pyruvate
■ This is regenerated through conversion of pyruvate to either ethanol
(alcoholic fermentation) or lactic acid (lactic acid fermentation)
■ This allows for regeneration of NAD+ to continue the glycolytic cycle

25
Q

Describe the coordinated regulation of glycolysis and gluconeogenesis.

A

○ Reciprocal regulation
■ within a cell, one pathway is relatively inactive while the other one is
highly active
■ when glucose is abundant, glycolysis will predominate. When glucose is
scarce, gluconeogenesis will take over

26
Q

Explain why the reaction catalyzed by the PDH complex is a
crucial juncture in metabolism.

A

Commits the carbon atoms of carbohydrates to oxidation by
the citric acid cycle or to the synthesis of fatty acids

27
Q

Identify the means by which the PDH complex is regulated.

A

Products of the PDH complex inhibit its activity (acetyl-CoA
and NADH), either directly, or through activation of pyruvate
dehydrogenase kinase

28
Q

Identify the primary catabolic purpose of the citric acid cycle.

A

Harvesting of high-energy electrons from carbon fuels.

29
Q

Explain the advantage of the oxidation of acetyl CoA in the citric acid cycle.

A

Harvesting of high-energy electrons from carbon fuels.

30
Q

Describe how the citric acid cycle is regulated.

A

There are three TCA enzymes that are highly regulated

31
Q

Explain the benefits of having the electron-transport chain located in a
membrane.

A

Allows for build up of proton gradient, so that proton-motive force can be
used to generate ATP

32
Q

Identify the ultimate determinant of the rate of cellular respiration.

A

Need for ATP

33
Q

Explain the regulation of glycogen breakdown.

A

Hormonal regulation by glucagon (pancreas) and epinephrine
(adrenal gland)

34
Q

Describe the steps of glycogen synthesis and identify the enzymes
required.

A

Glycogen synthase, Branching enzyme

35
Q

Identify the repeated steps of fatty acid degradation.

A

2 carbons at a time
oxidation, hydration, oxidation, thiolysis

36
Q

Explain how fatty acids are synthesized.

A

■ Citrate shuttle (oxacloacetate shuttle) in and out of mitochondria
■ Conversion of acetyl-CoA to malonyl-CoA in cytoplasm (commit step)
■ Fatty acid is synthesized in a 5 step elongation cycle

37
Q

Describe the relation between triacylglycerol synthesis and phospholipid synthesis.

A

Both begin with the precursor phosphatidate (diacylglycerol 3-phosphate) in the endoplasmic
reticulum
■ Triacylglycerol primarily synthesized in the liver
■ Phospholipid synthesis requires the combination of a diacylglycerol with an alcohol

38
Q

Phosphatidic Acid Phosphatase (PAP, lipin 1) Is a Key Regulatory Enzyme in Lipid Metabolism

A

Controls the extent to which triacylglycerols are synthesized relative to phospholipids

39
Q

List the regulatory steps in the control of cholesterol synthesis.

A

○ Controlled by the transcription factor sterol regulatory element-binding protein (SREBP)
○ Translation is inhibited by nonsterol metabolites derived from mevalonate as well as by dietary
cholesterol
○ Degradation is stringently controlled via increasing concentrations of sterols such as cholesterol
○ Phosphorylation by the AMP-activated protein kinase decreases the activity of HMG-CoA reductase.

40
Q

carbon atoms of cholesterol are
derived from acetyl CoA in a three-stage synthetic process:

A
  1. Stage 1 is the synthesis of isopentenyl pyrophosphate, an
    activated isoprene unit that is the key building block of
    cholesterol. (cytoplasm)
  2. Stage 2 is the condensation of six molecules of isopentenyl
    pyrophosphate to form squalene. (ER)
  3. In stage 3, squalene cyclizes and the tetracyclic product is
    subsequently converted into cholesterol. (ER)
41
Q

Cholesterol and triacylglycerols are packaged into _____ _____ for transport through bodily fluids.

A

lipoprotein particles

42
Q

The lipoprotein protein
components (called apoproteins) have two roles:

A

solubilize hydrophobic lipids and contain cell-targeting signals

43
Q

Describe the fate of nitrogen that is removed when amino acids are used as fuels.

A

○ Nitrogen is removed in the form of ammonium ions
■ Some ammonium is used in biosynthesis of nitrogen compounds
■ Excess is converted into urea via the urea cycle and excreted in the urine

44
Q

Explain how the carbon skeletons of the amino acids are metabolized after
nitrogen removal.

A

○ They are converted into glucose or acetyl-CoA

45
Q

Glucogenic amino acids

A

converted into pyruvate and will feed
into gluconeogenesis to produce
glucose.

46
Q

Ketogenic amino acids

A

converted into acetyl-CoA, the
precursor to ketone bodies.

47
Q

Identify the sources of carbon atoms for amino acid synthesis

A

intermediates of glycolysis, the
citric acid cycle, or the pentose phosphate pathway

48
Q

Identify the two stages of the pentose phosphate pathway

A

○ The oxidative generation of NADPH.
○ The nonoxidative interconversion of sugars

49
Q

Identify the enzyme that controls the pentose phosphate pathway.

A

Glucose 6-phosphate dehydrogenase

50
Q

Pentose Phosphate Pathway

A

Ribulose 5-phosphate is converted into ribose 5-phosphate
In the nonoxidative phase, the
pathway catalyzes the interconversion of three-, four-, five-,
six-, and seven-carbon sugars in a series of nonoxidative
reactions
Excess ribose 5-phosphate formed by the pentose
phosphate pathway can be completely converted into
glycolytic intermediates (fructose 6-phosphate and
glyceraldehyde 3-phosphate)