Cycle 3 BMP Workshop Flashcards

(55 cards)

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
# Define: Active site
Area on an enzyme that binds the substrate
26
How is the active site found?
Discovered by looking at enzyme's 3D shape, not primary structure
27
# True or False: The active site of an enzyme is only functional as tertiary structure
True
28
# Describe: The Catalytic Cycle
* The enzyme and substrate bind to form the ES complex * The complex becomes enzyme and product * The enzyme continues binding with substrate
29
What does extreme temperature do to enzymes? How is this dealt with?
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
What dictates an enzyme's optimum temperature?
The organism's environment
31
What are the types of membrane-bound proteins and how are they different?
* Integral vs. Peripheral membrane proteins * Differences in mobility
32
# State and describe: Types of membrane transport
* Passive: Follow their concentration gradients, spontaneous, increase in entropy * Active: Move against concentration gradients
33
# Explain: Passive transporter
* 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
# Explain: Active transporter
* 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
What does normal lung physiology involve?
A delicate balance of ions and water
36
What maintains the correct concentration gradient of chloride within the lungs
Chloride pump (CFTR), an ABC
37
Why does the lung require a concentration gradient of chloride?
Ensures correct osmosis of water, as water is needed to keep cilia wet and mobile to prevent lung infections
38
What prevents misfolded CFTR from reaching the membrane?
HSP90
39
# True or False: HSP90 is useful
Conditional. HSP90 is useful in health people, but it causes problems in cystic fibrosis (infections, thick mucus, troubles breathing)
40
What does the degree of lipid saturation affect?
The fluidity of the membrane * Increased stauration = decreased fluidity * Decreased saturation = increased fluidity
41
# Define: Desaturases
Enzymes that can adjust membrane fluidity by increasing the degree of unsaturation in membrane fatty acids
42
# True or False: Organisms cannot alter membrane fluidity
False, organisms can alter their membrane fluidity at different temperatures by changing the level of desaturase expression
43
# State: Components of phospholipids
1. Glycerol head (hydrophilic) 2. Fatty acid tails (hydrophobic
44
State the term for hydrophilic and hydrophobic domain together
Amphipathic
45
# State: Membrane permeability for different molecules
* Passive diffusion: Nonpolar molecules (lipids), small polar molecules (water) * Facilitated diffusion: Big polar molecules (glucose), ions (Cl-, Na+...)
46
# Define: Facilitated diffusion
Requires membrane proteins specific to the molecule
47
What are integral proteins?
Proteins that act as channels spanning the phospholipid bilayer
48
# Define: Hydropathy Plot
A graph where: * X-axis: Amino acid number * Y-axis: Relative hydrophobicity index * (Positive Y is hydrophobic, negative y is hydrophilic)
49
# True or False: Integral membranes have hydrophobic parts
True
50
# Explain: How proteins get on the plasma membrane or secreted out of cell
1. Endoplasmic reticulatum 2. Golgi apparatus 3. Plasma membrane via vesicles
51
Where does translation occur?
Cytoplasm
52
How is a protein sent to the membrane?
* A "tag" on the protein * Cell is able to recognize this tag * Cell transports proteins to proper places
53
# State: The steps of the Secretory Pathway
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
# True or False: The signal sequence is not included in mRNA
False, the signal sequence is included in the mRNA
55
Does the signal sequence appear in the initial protein? Final/mature protein?
The signal sequence appears as a polypeptide in the initial protein, but is excised in the final/mature protein