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BIO152 - cell bio > mse > Flashcards

mse Flashcards

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1
Q

precipiation of proteing at their isoelectric point is due to which of the following event?

A

proteins achieving a zero nett charge.

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2
Q

Keq is the equilibrium constant of an enzymatic reaction where the amount of
substrate A and product B are equilibrated after a period of time in a reversible
reaction. Which of the following options is incorrect?

A

Keq = [B].[A]

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3
Q
  1. An animal cell that lacks carbohydrates on the external surface of its plasma
    membrane would likely be impaired in which of the following functions?
A

b. Cell-cell recognition.

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4
Q

Which of the following statements correctly describes the property of hydrophobic
substances such as vegetable oil?

A

Nonpolar substances that repel water molecules

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5
Q

Fatty acids are ___________.

A

long, unbranched hydrocarbon chains

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6
Q

The conversion of NAD+ to NADH depicted is classed as what type of chemical
reaction?

A

reduction

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7
Q

a-ketoglutarate -> x -> succinate

= whats the name of metabolite X in the above reaction

A

succinyl CoA

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8
Q

The TCA cycle generates NADH and FADH2. What is the ATP yield generated from
each molecule in the mitochondria?

A

NADH: 3 ATP and FADH2: 2 ATP

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9
Q

In the glycerol phosphate shuttle, which of the following molecules is reduced to
transfer electrons into the mitochondria

A

DHAP (dihydroxyacetone phosphate)

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10
Q

Which one of the following enzymes is unique to gluconeogenesis

A

Pyruvate carboxylase

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11
Q

saturated fatty acids have…

A

single bonds, packed tightly, solidify at room temp

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12
Q

unsaturated fatty acids

A

double bonds= bends/kinks chain

do not pack tightly
remains liquid at rt

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13
Q

list inhibitors of the etc

A

Cyanide, azide, hydrogen sulphide, carbon monoxide
* React with cytochrome (a + a3) and prevent electron transfer to O2
* Antimycin
* Blocks electron flow from cytochrome b to c1
* Rotenone
* Inhibits NADH oxidoreductase
* Oligomycin
* Potent inhibitor of ATP synthase
* Atractyloside (from Mediterranean thistle)
* A toxic glycoside
* Inhibits translocase proteins

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14
Q

Each glucose that is metabolised by glycolysis generates a net gain of four ATP.

Is this statement true or false?

A

false

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15
Q

How efficient is the trapping of energy from glycolysis?

A

30%

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16
Q

The TCA cycle generates NADH and FADH2 but how many of each are produced from one pyruvate molecule?

A

4 NADH and 1FADH2

17
Q

The equivalent of only one ATP is directly trapped by substrate-level phosphorylation by the TCA cycle.

Is this statement true or false?

A

true

18
Q

In muscle cells, glucose is metabolised to pyruvate. Under anaerobic conditions, this pyruvate is then converted to lactate. Why?

A

It re-oxidizes the cytoplasmic NADH generated by glycolysis

19
Q

During glycolysis, NADH is formed in the cytoplasm. Under aerobic conditions, what is the fate of this NADH?

A

It is re-oxidised to NAD+ by the glycerol-3-phosphate shuttle

20
Q

The ATP yield from 1 mitochondrial NADH under aerobic conditions in a eukaryotic cell would be

A

3 ATP

20
Q

Respiratory control is the mechanism that ensures that the electron transport chain is not active unless ____
is needed by the cell

A

ATP

21
Q

ATP synthesis by ATP synthase is powered by a ____ gradient.

A

proton

22
Q

In the electron transport chain, cytochrome b transfers its electrons to which compound?

A

Cytochrome c1

23
Q

Glucose and galactose yield the same amount of ATP when they feed into glycolysis. True or false?

A

true

24
Q

describe the difference between catabolism and anabolism.

A

Catabolism
- Degradative reactions of metbolism
- Larger compounds are broken down into smaller ones generating energy

Anabolism
- Synthetic (building) reactions of metabolism
- Smaller compounds are combined into larger ones
- Requires energy

25
Q

Distinguish between the reaction types of the seven major classes of enzymes

A

Class1: oxidoreductase
Reaction : catalyses redox reactions (transfer og H O or e-)
Example : alcohol, dehydrogenase

Class 2: transferase
Reaction: transfer a functional groun from one molecule to another
Example ; hexokinase

Class 3: hydrolase
Reaction: hydrolase (breaks bonds) in presence of water
Example: glucose-6-phosphatase

Class 4: lyase
Reaction: remove or add groups to a molecule (breaks bonds, electron rearrangement)
Example: pyruvate, decarboxylase

Class 5: isomerase
Reaction: rearrange functional groups in a molecule (isomers)

Class 6: ligase
Reaction: join molecules
Example: pyruvate, carboxylase

Calss 7: translocases
Reaction: catalyses movement of ions/molecules across membrane
Example: sodium-potassium ATPase pump

26
Q

how to differenciate between rogh and smooth ER

A

rough is ribosome dotted

27
Q

what do lysosomes do

A
  • Single membrane bouns vesicle produced from golgi complex
  • Functions:
     Stores enzyme (lysozyme, hydrolase
     Destroys lyses material in vesicles
     Breakdown macromolecules (proteins)
     Recycles cell contents (aging organelles)
28
Q

LLO1.5 Distinguish plant cells from animal cells based on their cellular features

A

Things that plant cels have that animals do not:
Cell wall
- Provides structural support
- Made up of cellulose microfibrils in a matrix of polysaccharides and proteins
 Flexible and extensible
- Cell walls connected by plasmodesmata (openings)
 Membrane lined
 Allows for water and small solutes to pass
Chloroplast
- Inner and outer membrane
- Third membrane system
 Granum: stacks of flattened sacs called thylakoids
 Tubular membranes: stoma thylakoids which connects sacs together
- Functions:
 Site of photosynthesis (in stroma)
 Light driven process( solar energy and CO2)
 Produce sugar and organic compounds
Vacuoles
- Single membrane bound
- Function:
 Temporary storage and transport
 Phagocytosis
 Storage and intracellular digestion
 Maintains turgor pressure

Peroxisomes
- Specialized peroxisomes: Glyoxysomes
 Crystalline core: enzyme catalase

 Germination: converts fats into carbs
Involves in photorespiration

29
Q

draw an amino acid

A
  • Made up of
     A (alpha) carbon
     Hydrogen atoms
     Carboxyl group (carboxylic acid) (COO)
     Amino group (Amine( NH3)
     R group
30
Q

non polar aa are hydrophobic r hydrophillic

A

hydropobic

31
Q

describe the primary structure of a protein

A
  • Linear sequence of aa in polypeptide
     Aa linked by peptide bonds
  • Sequence determines higher order of structures
32
Q

describe the secondary structure of a protein

A

Secondary structure
- Backbone of polypeptide
 Linear sequence fold upon itself
- Structure stabilized by H bonds
 Intermolecular (between CO and NH groups of AA of 2 different poly peptides)
 Intramolecular (between CO and H+NH groups of aa of the SAME poly peptide
- Structural patterns
 A heliex

 B sheet

Motifs
- Combinations of a helices and b sheets
 Connected via looped regions varying lengths (random coils)
 Examples B-a-B , hairpin loop and heliet turn heliec motifs

33
Q

describe the tertary structure of a protein

A

Tertiary structure
- Higher order of folding
 Poly peptide chain folded back on itself to form a condensed structure
 Depends on interation between the side chains
-
- Stabilized by
 Disulphide bonds
 Hydrogen bonds
 Ionic bonds
 Van der Waals interaction
 Hydrophobic interaction
- Two main classes
 Fibrous protein vs globular proteins

34
Q

describe the quaternary structure

A
  • Between multile polypeptides
  • Held together by same bonds of tertary structure
  • Example :HAemagblobin
     Multimeric protein = tetramer
     = 4 polypeptides= 2a and 2b subunits
35
Q

Describe how pH that affects the charge of proteins

A

pH affects proteins by changing the protonation state of the charged residues
- affects H+ bonds and ionic bonds
Acid
- Low pH
- Increase H+
- + charge

Neutral
- Uncharges
- Isoelectric point/pI

Alkaline/ basic
- High pH
- Decreased H+
- - charge

36
Q

Describe what denaturation does to the protein structure

A

Protein denaturing
- Structures must be maintained for biological function
- Agents may casue loss of structures (2 (secondary), 3 (tertiary) and/or 4 (quaternary) by disrupting bonds
- Loss of structure + function= denaturation
Factors causing denaturation
- Organic solvents- disrupts H bonds (2,3,4)
- Detergents – distrupts hydrophobic bonds (3,4)
- pH extremes – disrupts H bonds (,3,4) and ionic (electrostatic) bnds (3,4)
- heat – increase kinetic energy and disrupts all non-covalent bonds (2,3,4)

37
Q

Describe the types of lipids and proteins in membranes

A
  1. Phospholipids (most abundant)
    - Consists of a back bone
    - They have a polar head: contains phosphate group variable R group such as chlorine and is charged so therefore hydrophilic (polar)
    - Backbone = glycerol and sphingosine
    - Non-polar tails: fatty acids, long unbranched hydrocarbon chain with arbon,y grounp
    - Saturated or unsaturated
    - Hydrophobic
  2. Glycolipids
    * Lipid with carbohydrate group
    * E.g., Glycoglycerolipids & glycosphingolipids
  3. Sterols
    * Have four-ringed hydrocarbon
    * E.g., Cholesterol & phytosterol (plant)

BIO152 - cell bio (10 decks)

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