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MCAT Miscellaneous > Review 3 > Flashcards

Review 3 Flashcards

1
Q

Line-Weaver Burke plot Equation

A

1/V0 = (Km/Vmax)(1/[S]) + 1/Vmax

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2
Q

Competitive Inhibition

A
  1. E + S (Binds to E)
  2. Apparent increase in Km and does not affect Vmax
  3. Increased [S] can overcome inhibition
  4. Think of the graph
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3
Q

Uncompetitve inhibition

A
  1. ES (Binds to the transition state)
  2. Apparent increase in 1/Vmax but decrease in Vmax (Because always stuck in transition state and not product formation)
  3. Increased [S] will not do anything lol
  4. Think of the graph
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4
Q

Non-competitive Inhibition (Mixed)

A
  1. E + S (Can bind here) and ES (can bind here)
  2. Apparent increase in Km and in 1/Vmax but decrease in Vmax
  3. Increased [S] does not relieve anything
  4. Think of the graph
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5
Q

Km

A

Think (k-1 + k2)/k1 => (Loss of [ES]/Formation of [ES] and that denominator is the key to explaining everything

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6
Q

Positive Cooperativity

A

Substrate binding increases affinity for subsequent substrate (Affect Km)

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7
Q

Negative Cooperativity

A

Substrate binding decreases affinity for subsequent substrate (Affect Km)

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8
Q

Non-cooperative Binding

A

Substrate binding DOES NOT AFFECT affinity for subsequent substrate (Affect Km)

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9
Q

Allosteric Activator

A

Binding increases enzymatic activity. The affect the Km

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10
Q

Allosteric inhibitor

A

Binding decreases enzymatic activity (Affect Km)

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11
Q

Feedback Loop effects

A
  1. Positive increase the rate

2. Negative loops decrease the rate

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12
Q

Homotropic vs. Heterotropic

A

Former the regulating molecule is a substrate of the enzyme

Latter the regulating molecule is not the substrate of the enzyme

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13
Q

Small Post-translational modifications to Enzymes

A
  1. Methylation (-CH3)

2 Acetylation (CH3-C=O)

  1. Glycosylation
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14
Q

Zymogens

A

Inactive enzymes that require covalent modifications

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15
Q

Enzyme Inhibition

A
  1. Uncompetitive
  2. Competitive
  3. Non-competitive (Mixed)
  4. Suicide (covalent) inhibition
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16
Q

Cholesterol, Unsaturated, and Saturated Fats

A

Cholesterol - Increase fluidity at low temperatures and decreases fluidity at high temperature

Unsaturated - Decrease fluidity

Saturated - increase fluidity

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17
Q

Mixed Inhibition

A
  1. E + S (Can bind here) and ES (can bind here)
  2. Apparent increase in Km and in 1/Vmax but decrease in Vmax
  3. Increased [S] does not relieve anything
  4. Think of the graph.
  5. The difference between non-competitive and mixed inhibition is that mixed inhibition binds to either the enzyme or the enzyme-substrate complex but has different affinities for each
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18
Q

Coenzymes

A

These are ORGANIC non-protein molecules that bind to proteins and are required for their function

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19
Q

Cofactors

A

These are INORGANIC non-protein molecules that bind to proteins and are required for their function

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20
Q

Apoenzymes

A

These are enzymes without their cofactors

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21
Q

Holoenzymes

A

These are enzymes with their cofactors

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22
Q

Cosubstrate

A

They reversibly bind and transfer chemical group

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23
Q

Prosthetic group

A

The molecule covalently bound to an enzyme

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24
Q

Oxidoreductase

A

Oxidation-reduction. Transfer electrons of hydrogen ions (oxidase, reductase, dehydrogenase)

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25
Q

Transferase

A

Groups are transferred from one location to another (aminotransferase, kinase)

26
Q

Kinase

A

Transfers a phosphate group from ATP or other high energy carrier to a substrate

27
Q

Phosphorylase

A

Catalyzes the addition of a phosphate group from an inorganic phosphate to a substrate

28
Q

Hydrolase

A

Hydrolysis reactions (ATPase, protease, nuclease, lipase)

29
Q

Protease

A

Hydrolyses peptide bonds (trypsin, chymotrypsin, pepsin)

30
Q

Phosphatase

A

Removes phosphate groups from a molecule

31
Q

Lyase

A

Catalyzes the cleavage of a bond or the synthesis (synthase) of a bond without the addition of an outside molecule (like water). Often forms or breaks double bonds

32
Q

Ligase

A

Catalyzes condensation reactions with the hydrolysis of high energy molecule. Usually

33
Q

Cytoskeleton

A

Intracellular scaffolding anchored to cell membrane to provide support and organization

34
Q

Matrix

A

Extracellular support the tissue of the body (tendons, ligaments, cartilage, basement membrane)

35
Q

Elastin

A

Tri-helical fiber and makes up most of the extracellular matrix, important for
strength and flexibility. Major component of the bone

36
Q

Collagen

A

Extracellular, stretches and recoils like a spring, restores original shape of tissue

37
Q

Keratin

A

Intermediate filaments found in epithelial cells. Functions to waterproof and strengthen the tissue. Found in hair and nails

38
Q

Actin

A

Intracellular, make up of microfilaments and the thin filaments in myofibrils. Most abundant protein in eukaryotic cells.

39
Q

Tubulin

A

Intracellular, make up mictrotubules. Provide structure, chromosome separation in mitosis and intracellular transoirt with kinesin and dynein

40
Q

Kinesin

A

Positive end. They align chromosomes during metaphase, brings vesicles to membrane (neurotransmitters release)

41
Q

Dynein

A

Negative end. The sliding movement of cilia and flagella, takes vesicles away from membrane (neurotransmitters reuptake)

42
Q

Binding Proteins

A

Bind and transport or sequester molecules (hemoglobin, calcium binding protein, transcription factors)

43
Q

Call Adhesion Molecules

A

They can be found on the surface of most cells and aid in the binding of the cell to the extracellular
matrix of other cells. Integral Membrane Proteins

44
Q

Cadherins

A

They are glycoproteins involved in calcium-dependent adhesion. They hold similar types of cells together
(epithelial)

45
Q

Integrins

A

They span both membranes, bind to and communicate with extracellular matrix and cellular signaling. They promote cell division, apoptosis, white blood migration, clotting.

46
Q

Selectins

A

They weakly bind to carbohydrate molecules that project from other cell surfaces. They are expressed on white blood cells. They play a role in host defense, inflammation, and white cell migration.

47
Q

G-Protein Linked Receptor Mechanism

A
  1. Epinephrine arrives at the cell surface and binds to a specific G-protein linked receptor
  2. The cytoplasmic portion of the receptor activates G-proteins, causing GDP to dissociate and GTP to bind in its place
  3. The activated G-proteins diffuse through the membrane and activate adenylyl cyclase
  4. Adenylyl cyclase makes cAMP from ATP
  5. cAMP activates cAMP-dependent protein kinases (cAMP-dPK) in the cytoplasm.
  6. cAMP-dPK phosphorylates certain enzymes, with the end result being mobilization energy. For example, enzymes necessary for glycogen breakdown will be activated, while enzymes necessary for glycogen synthesis will be inactivated, cAMP-dPK phosphorylation.
48
Q

G-Protein Linked receptor Function

A

G-protein-linkedreceptoractivatesmanyG-proteins,eachG-proteinactivatesmanyadenylyl cyclase enzymes, each adenylyl cyclase makes lots of cAMP from ATP, each cAMP activates many cAMP-dPK, and each cAMP-dPK phosphorylates many enzymes

49
Q

G-Protein Linked receptor basic process

A
  1. Ligand binds receptor
  2. Receptor exchanges GDP to GTP
  3. G protein becomes activated
  4. G protein either activates or inactivates target protein
  5. G protein hydrolyses GTP to GDP
  6. G protein becomes inactivated
50
Q

Native Page

A
  1. Separates by mass to charge ratio.

2. Useful to compare size of charged proteins with similar size.

51
Q

SDS-PAGE

A
  1. Separates based on mass only

2. SDS a detergent that disrupts all noncovalent bonds and binds to protein giving it a negative charge.

52
Q

Isoelectric focusing

A
  1. Separates based on pI
  2. Gel has a pH gradient ( acidic at the anode, basic at the cathode)
  3. Proteins that are positively charged will begin migrating toward the CATHODE and proteins that are negatively charged will begin migrating toward the ANODE.
  4. When the protein reaches the portion of gel where the pH = pI, the protein takes on a NEUTRAL charge and will STOP.
53
Q

Chromatography

A
  1. The more similar the compound is to its surroundings (by polarity, charge, and so on), the MORE it will stick to its surrounding and SLOWER it will move.
  2. Chromatography is preferred over electrophoresis if LARGE amounts of protein are being separated.
54
Q

Stationary Phase

A

Can be charged, have pores or special affinities.

55
Q

Column Chromatography

A

Polar silica or alumina beads, the more polar the protein, the SLOWER it will move

56
Q

Ion-Exchange Chromatography

A
  1. Beads coated with charged substances
  2. A positively charged column will attract and hold a negatively charged protein as it passes though the column, INCREASES its retention time
57
Q

Cation Exchange

A

Bind positively charged molecules

58
Q

Anion Exchange

A

Bind negatively charged molecules

59
Q

Size-exclusion Chromatography

A

beads have tiny pores which allow small compounds to enter slowing them down, large proteins can’t fit into pores and therefore the LARGE proteins will elute first

60
Q

Affinity Chromatography

A
  1. Columns to bind any protein of interest by creating a column with high affinity.
  2. Use receptors or substrate for the protein, antibodies
61
Q

Protein Structure

A

X-ray Crystallography and NMR Spectroscopy

62
Q

Amino Acid Composition

A
  1. Hydrolysis followed by chromatography
  2. Edmans degradation sequences by selectively removing amino acids of the proteins from the N-terminal
    which can be analyzed by mass spectroscopy.

MCAT Miscellaneous (17 decks)

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