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My Packs: UWO (BIO 1002) > Cycle 3 BMP Workshop > Flashcards

Cycle 3 BMP Workshop Flashcards

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Biology 101 flashcards
1
Q

List and Describe:

Types of energy

A
  1. Kinetic: From moving particles
  2. Potential: “Stored” by position or chemical structure
  3. Chemical: From chemical reactions
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2
Q

List and explain:

Types of systems

A
  1. Open: Exchange matter AND energy (e.g. cells)
  2. Closed: Exchange energy only
  3. Isolated: Neither
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3
Q

List and explain:

The first two laws of thermodynamics

A

Law 1: Energy CANNOT be made or destroyed, it can only be converted

Law 2: Entropy (“disorder”) of the universe ALWAYS INCREASES

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4
Q

How do cells fight the 2nd Law of Thermodynamics?

A

Cells use energy to build “ordered” molecules
They are “islands” of low entropy (energy taken in to replace other things broken down)

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5
Q

State:

The levels of protein structure

A
  1. Primary (denatured)
  2. Secondary
  3. Tertiary (functional proteins)
  4. Quaternary (functional proteins)
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6
Q

Describe the structure and bonding of:

Primary structure protein

A
  • Unfolded, 1 linear chain of amino acids
  • Peptide bonds joining amino acids
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7
Q

Describe the structure and bonding of:

Secondary structure protein

A
  • 1 chain of amino acids (alpha-helix form or beta-barrel form)
  • Peptide + Hydrogen bonds
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8
Q

What are hydrogen bonds disturbed by?

A

Urea

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9
Q

Describe the structure and bonding of:

Tertiary structure protein

A
  • 1 fully folded 3D chain
  • Peptide, Hydrogen + any other bond (dipole-dipole, disulfide bridges etc.)
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10
Q

Describe the structure and bonding of:

Quaternary structure protein

A
  • Multiple fully folded 3D chains
  • Peptide, Hydrogen + any other bond (dipole-dipole, disulfide bridges etc.)
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11
Q

Describe:

Most reduced molecules

A
  • More C-H bonds
  • HIGH free energy
  • Electrons are easy to remove
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12
Q

Describe:

Most oxidized molecules

A
  • More C-O bonds
  • LOW free energy
  • Electrons are more tightly bound to oxygen
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13
Q

Explain:

Heterotrophs

A
  • “We like, we want”
  • Consume: Matter and energy combine through our carbs + fats
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14
Q

Explain:

Autotrophs

A
  • “We hate, we expel”
  • Consume matter (CO2) and energy (light)
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15
Q

State the type of equation and explain:

The values in the equation:
ΔG = ΔH - TΔS

A

Thermodynamic Equation
* ΔG: Free energy, = Products - Reactants
* ΔH: Enthalpy
* ΔS: Entropy

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16
Q

State the meaning of:

ΔG > 0
ΔG < 0

A

Free Energy
* ΔG > 0: Endergonic, requires energy
* ΔG < 0: Exergonic, spontaneous

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17
Q

State the meaning of:

ΔH > 0
ΔH < 0

A

Enthalpy
* ΔH > 0: Endothermic
* ΔH < 0: Exothermic

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18
Q

State the meaning of:

ΔS > 0
ΔS < 0

A

Entropy
* ΔS > 0: More spread out (less order)
* ΔS < 0: Less spread out (more order)

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19
Q

What do enzymes do?

A

Enzymes LOWER ACTIVATION ENERGY to speed up the reaction

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20
Q

True or False:

Enzymes change ΔG

A

False

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21
Q

True or False:

Enzymes do not give energy

A

True

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22
Q

What is required for endergonic reactions to occur?

A

Energy providers (e.g. ATP)

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23
Q

True or False:

Unfolded protein (primary structure) is very stable

A

False, unfolded proteins have high ΔG, making it very unstable

24
Q

Explain:

The Energy Funneling Process

A
  • Multiple ways to fold a protein from primary structure
  • There may be transitional/misfolded proteins along the way
  • Chaperones use energy to get proteins to unfold and refold correctly
  • The final active protein has low ΔG, making it most stable
25
Q

Define:

Active site

A

Area on an enzyme that binds the substrate

26
Q

How is the active site found?

A

Discovered by looking at enzyme’s 3D shape, not primary structure

27
Q

True or False:

The active site of an enzyme is only functional as tertiary structure

A

True

28
Q

Describe:

The Catalytic Cycle

A
  • The enzyme and substrate bind to form the ES complex
  • The complex becomes enzyme and product
  • The enzyme continues binding with substrate
29
Q

What does extreme temperature do to enzymes? How is this dealt with?

A

Extreme cold causes enzyme to become too rigid
* “Weaker” tertiary structure bonds or arrangements to allow enzyme to be fluid

Extreme heat causes enzyme to become too fluid (denatures)
* “Stronger” tertiary structure bonds or arrangements to allow for more rigid enzyme

30
Q

What dictates an enzyme’s optimum temperature?

A

The organism’s environment

31
Q

What are the types of membrane-bound proteins and how are they different?

A
  • Integral vs. Peripheral membrane proteins
  • Differences in mobility
32
Q

State and describe:

Types of membrane transport

A
  • Passive: Follow their concentration gradients, spontaneous, increase in entropy
  • Active: Move against concentration gradients
33
Q

Explain:

Passive transporter

A
  • The passive transporter acts as a hole in the membrane for the particle to pass through
  • The membrane prevents movement of the particle; if there was no membrane, the particle would move in this way
34
Q

Explain:

Active transporter

A
  • Using ATP (energy) to move the particle, as without ATP, the reaction would be endergonic and non-spontaneous
  • If there was no membrane, the particle would move in a manner opposite to this
35
Q

What does normal lung physiology involve?

A

A delicate balance of ions and water

36
Q

What maintains the correct concentration gradient of chloride within the lungs

A

Chloride pump (CFTR), an ABC

37
Q

Why does the lung require a concentration gradient of chloride?

A

Ensures correct osmosis of water, as water is needed to keep cilia wet and mobile to prevent lung infections

38
Q

What prevents misfolded CFTR from reaching the membrane?

A

HSP90

39
Q

True or False:

HSP90 is useful

A

Conditional.
HSP90 is useful in health people, but it causes problems in cystic fibrosis (infections, thick mucus, troubles breathing)

40
Q

What does the degree of lipid saturation affect?

A

The fluidity of the membrane
* Increased stauration = decreased fluidity
* Decreased saturation = increased fluidity

41
Q

Define:

Desaturases

A

Enzymes that can adjust membrane fluidity by increasing the degree of unsaturation in membrane fatty acids

42
Q

True or False:

Organisms cannot alter membrane fluidity

A

False, organisms can alter their membrane fluidity at different temperatures by changing the level of desaturase expression

43
Q

State:

Components of phospholipids

A
  1. Glycerol head (hydrophilic)
  2. Fatty acid tails (hydrophobic
44
Q

State the term for hydrophilic and hydrophobic domain together

A

Amphipathic

45
Q

State:

Membrane permeability for different molecules

A
  • Passive diffusion: Nonpolar molecules (lipids), small polar molecules (water)
  • Facilitated diffusion: Big polar molecules (glucose), ions (Cl-, Na+…)
46
Q

Define:

Facilitated diffusion

A

Requires membrane proteins specific to the molecule

47
Q

What are integral proteins?

A

Proteins that act as channels spanning the phospholipid bilayer

48
Q

Define:

Hydropathy Plot

A

A graph where:
* X-axis: Amino acid number
* Y-axis: Relative hydrophobicity index
* (Positive Y is hydrophobic, negative y is hydrophilic)

49
Q

True or False:

Integral membranes have hydrophobic parts

A

True

50
Q

Explain:

How proteins get on the plasma membrane or secreted out of cell

A
  1. Endoplasmic reticulatum
  2. Golgi apparatus
  3. Plasma membrane via vesicles
51
Q

Where does translation occur?

A

Cytoplasm

52
Q

How is a protein sent to the membrane?

A
  • A “tag” on the protein
  • Cell is able to recognize this tag
  • Cell transports proteins to proper places
53
Q

State:

The steps of the Secretory Pathway

A
  1. RNA translated by ribosome, and a signal sequence pops out as polypeptide
  2. Translation stops. Signal receptor protein (SRP) binds to signal sequence
  3. SRP binds to a SRP receptor protein on the ER. Translation continues into the ER
  4. Following translation of protein to be sent to the membrane, the signal sequence is cut
54
Q

True or False:

The signal sequence is not included in mRNA

A

False, the signal sequence is included in the mRNA

55
Q

Does the signal sequence appear in the initial protein? Final/mature protein?

A

The signal sequence appears as a polypeptide in the initial protein, but is excised in the final/mature protein

My Packs: UWO (BIO 1002) (10 decks)

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