Cell chemistry and Bioenergetics Lectures Flashcards

1
Q

What are the properties of chemical bonds?

A
  • Bond strength -> amount of energy needed to break it
  • Covalent bonds are 100x stronger than non-covalent bonds
  • Covalent bonds form macromolecules
  • Covalent bonds resist being pulled apart by thermal motions
  • Covalent bonds only broken by biologically catalyzed chemical reactions
  • Non-covalent bonds allow molecules to recognize each others and reversible associate
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2
Q

Describe the chemical components of the cell?

A
  • 99% total number of atoms in the cell: C, H, N, O’
  • 0.9% total number of atoms in the cell: P, S, Cl, Na, Mg, K, Ca

Popular Combinations:
- Methyl (CH3)
- Hydroxyl (-OH)
- Carboxyl (-COOH)
- Carbonyl (C=O)
-Phosphate (-PO3^-2)
- Suflhydryl (-SH)
- Amino (-NH2)

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3
Q

How are cell compounds formed?

A
  • Carbon atoms can form four covalent bounds with other atoms -> high ability to form macromolecules
  • C-C stable bonds form chains and rings -> generate large and complex molecules
  • Carbon compounds made by cells -> organic compounds
  • A few categories of molecules give rise to all extra extraordinary richness of form and function
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4
Q

Where are organic compounds found? What are they based with?

A
  • They are carbon based (around 30 carbons)
  • They are found in free solution
  • Compounds in the cell are chemically related and classified in 4 major families of compounds
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5
Q

What are the uses of organic compounds?

A

1) Monomer subunits to construct Polymeric Macromolecules

2) Energy sources -> broken down and transformed into other small molecules (used in metabolic pathways)

3) Many have both functions (subunits and energy sources)

4) Organic molecules are synthesized or broke down into the same set of simple compounds

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6
Q

What macromolecules do the following organic compounds form:
1) Sugars
2) Fatty Acids
3) Amino Acids
4) Nucleotides

A

1) Polysaccharides, glycogen and starch (in plants)

2) Fats and membrane lipids

3) Proteins

4) Nucleic Acids

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7
Q

What is a macromolecule?

A
  • Most abundant carbon containing molecules
  • Principle building and functional blocks of cells
  • Made by covalently linked organic molecules (monomers) into chains
  • Sugar/amino acid: versatile and perform thousands of functions, Enzymes catalyze formation and breaking of covalent bonds
  • Nucleic acid -> DNA and RNA
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8
Q

How do macromolecules assemble?

A

The subunits are added in a precise order and they are very organized to account for specific conformation anf function.
The covalent bonds are flexible and rotate - there are several different conformations.
There are not several different conformations for non-covalent bonds.
Non-covalent bonds allow macromolecules to interact with each other - they constrain shape to one conformation.

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9
Q

What are the two types of reactions for cell metabolism?

A

1) Anabolic Pathway: two monomers put together through covalent bonding - need to provide energy to make bonds.
Energetically unfavourable.

2) Catabolic Pathway: break bonds and make monomers - release energy when bonds are broken.
Energetically favourable.

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10
Q

What is the second law of thermodynamics?

A
  • In any isolated system the degree of disorder always increases. The mot probably arrangement is the most disorder (if there is no energy in the system)
  • Amount of disorder in any system is quantified and express as the ENTROPY (S) –> The greater the disorder the greater the entropy –> Systems will change spontaneously towards arrangements with Higher S.
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11
Q

How is it possible that the release of heat energy enables cell order?

A

You need to consider a cell a non-isolated system. It has an environment. Interactions inside the cell have order and also release heat to its environment. It warms up the environment. And when the liquid has heat, the molecules move faster and it creates disorder.

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12
Q

Where does the cell heat come from?

A

It comes from food.

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13
Q

What is the first law of thermodynamics?

A

The energy can be converted from one form to another but cannot be created or destroyed. In biological systems, energy is stores and managed with chemical bonds. A negative enthalpy change (Hf-Hi) spontaneously favorable reaction.

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14
Q

What is Gibbs free energy?

A

G = H-TS

  • Gibbs free energy, denoted G, combines enthalpy and entropy into a single value. The change in free energy, ΔG, is equal to the sum of the enthalpy plus the product of the temperature and entropy of the system.

PUTTING it all together!

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15
Q

What is the effect of enzymes in a reaction?

A

Enzymes catalyze the reaction by lowering the activation energy required for a reaction to take place. It then takes less time for the reactants to reach the required activation energy, therefore speeding up the reaction.
Enzymes speed up reactions but cannot force energetically unfavourable reactions to occur (cannot go uphill)

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16
Q

What is meant by “reaction in cells are coupled”?

A

There are two types of reactions, anabolic and catabolic. The energy in one reaction is used in another, they drive each other. They need carrier molecules to take energy and favour anabolic reactions. The main carrier in our cells is ATP.

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17
Q

What sign is Delta G going to be in order for cells to work?

A

Delta G has to be (-)

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18
Q

In cells, describe the concept of equilibrium:

A
  • Suppose there is a reaction between Y and X. In this example, the formation of X is energetically favoured in this example. The delta G of Y -> X is negative and the delta G of X -> Y is positive. Because of thermal bombardments, there will always be some X converting to Y and vice versa.
  • Suppose we start with an equal number of Y and X molecules, the conversion of Y to X will happen more often than the conversion of X to Y. Because one is energetically favoured over the other.
  • Eventually, there will be a large enough excess of X over Y to compensate for the slow rate of X -> Y. This is when equilibrium is attained.
  • At equilibrium, the number of Y molecules being converted to X molecules each second is exactly equal to the number of X molecules being converted to Y each second, there is no net ratio.
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19
Q

What is an example of a reaction driven by ATP hydrolysis?

A

A-OH + B-H —> A-B

Step 1)
Activation step, ATP transfers a phosphate P, to A-OH to produce a high-energy intermediate

A-OH ———> A-O-P (ATP in and ADP is released)

Step 2)
In the condensation step, the activated intermediate reacts with B-H to form the product A-B, a reaction accompanied by the release of inorganic phosphate.

A-O-P ———> A-B (B-H in, P out)

Net result)

A-OH + B-H + ATP —> A-B + ADP + P

20
Q

What is the most used activated carrier?

A

ATP

21
Q

What is Acetyl CoA?

A

It is a molecule that provides energy. You see it a bit less often. It is a high energy thioester bond which is used to transfer energy through reactions.

22
Q

How does oxidation and reduction involve electron transfer? What is the difference between the two?

A

1) Oxidation in cells –> Removal of electrons from an atom. Partially + charge.
When oxidized, carbon dioxide.

2) Reduction –> Addition of electrons to an atom. Partially - charge.
When reduced, methane.

23
Q

What is hydrogenation?

A

If a molecule picks an e^-, it also usually picks up an H.

24
Q

When would hydrogeneration = reduction?

A
  • If the number of C-H bonds increases, the molecule would be reduced.
  • In cells, reduction and hydrogenation is the same.
25
Q

What is NADH and NADPH?

A

When there is oxidation in a reaction, there are molecules that carry electron and hydrogen, and these molecules are called NADH and NADPH. They carry electrons and hydrogens.

26
Q

List what the following activated carries cary: (in high-energy linkage)
1) ATP
2) NADH, NADPH, FADH2
3) Acetyl CoA
4) Carboxylated biotin
5) S-Adenosylmethionine
6) Uridine diphosphate glucose

A

1) Phosphate
2) Electrons and hydrogens
3) Acetyl group
4) Carboxyl group
5) Methyl group
6) Glucose

27
Q

Why is diversity important in protein structure?

A

So they can perform many different important functions.

28
Q

How do proteins acquire function?

A

By folding into a 3-dimensional conformation. Folding provides physical stability and functional surfaces. The sequence of amino acids of a protein determines its structure, function and localization. Proteins are a sequence of Amino acids.
Nucleic acids function as lineal polymers and are translated by ribosomes.
Proteins are polymers made up of 20 different amino acids (monomer)
In centre there is a carbon that makes 4 covalent bonds to amino , carboxyl (acidic) and to X.

29
Q

Amino acids are joined together by an amide linkage called ____?

A

Peptide Bond

30
Q

What type of bonds are polypeptides made by?

A

Covalent bonds

31
Q

Describe the Polypeptide Backbone:

A

The peptide bond is planar and cannot rotate. Rotation around the bonds to the central carbon (Calpha) is possible. The polypeptide backbone has limited freedom of rotation. Some rotation angles between amino acid (residues) in a polypeptide are prefferes.

32
Q

What are3 types of non-covalent bonds?

A

Interactions between residues of a polypeptide stabilize structure.

1) Hydrogen bonds
2) Van der Waals interactions (transient dipoles between all atoms)
3) Ionic bonds

33
Q

What bonds are between cysteines? What proteins is this in?

A

-Disulfide Bonds
Secretory proteins often have covalent difulside bonds between cysteine side chains. There are extracellular proteins inside the secretory organelles. And disulfides reinforce this structure.

34
Q

What proteins do not have disulfide bonds and where?

A
  • Cytosolic proteins normally do not have disulfide bonds
    This is in the cytosol, nucleus and mitochondria.
35
Q

Describe the 4 organization levels that contribute to protein structure:

A

1) Primary structure - Linear Amino Acid sequence

2) Secondary structure - Local conformation patterns
Alpha helix: single polypeptide chain twist around itself.
- Backbone is coiled, hydrogen bonds between C=O and N-H formed every 4 peptide bonds in each turn of helix backbone, side chains point outwards.
Beta-sheets: neighbouring segments of the polypeptide backbone
- Backbone is extended almost straight, several strands pack sideways into a beta-sheet, hydrogen bonds between the backbone strands, side chains on alternate sides, very rigid, two types

3) Tertiary structure - complete three-dimensional arrangement of the polypeptide.
- Secondary structure elements are packed against eachother to form tertiary structure. Hydrophobic contacts between secondary elements. Long-range contacts between residues that are far apart in the primary sequence. Loops have no regular secondary structure so they can be flexible.

4) Quaternary structure - the assembly of multiple polypeptides (subunits) into a final protein.
- Interactions between subunits are very stable, dimer: two polypeptide subunits, trimer, tetramer, 5-mer, 6-mer etc. Oligomer: many subunits.

36
Q

What are 4 different representations to visualize proteins?

A

1) Polypeptide backbone

2) Ribbon diagram (polypeptide backbone only)

3) Stick diagram (include AA R chain)

4) Space-filling model (with mass of atoms)

37
Q

What is a domain?

A
  • A domain is an independently folded unit within a protein
  • Proteins can have one or multiple domains
  • Different domains in a protein have different functions
  • Each function of a domain is independent from another domain
38
Q

What is meant by “Domain Combinations”?

A
  • Some conserved domains are found in many different proteins, in combinations with other domains
  • These “modular” domains often form reversible, specific, non-covalent contacts with other molecules. Other proteins (different from quatermary structure), lipids, carbohydrates, RNA, DNA< other cofactors
39
Q

What is the length of a polypeptide?

A
  • Most human polypeptides are 100 to 800 amino acids long, or from 12 kDa to 90 kDa molecular weight
  • Domains are usually 50 to 200 amino acids long
  • Long proteins have multiple domains
40
Q

Are protein interactions often transient? What is meant by this?

A

Yes!
It means that interactions form and break apart quickly. Thermal motion means all molecules are constantly moving and tumbling, and colliding.

41
Q

What does sequence similarity indicate?

A

(homology) indicates evolutionary conservation.
It suggest a common structure or function.

42
Q

If polypeptides do not have sequence similarity, what are they considered to be?

A

Divergent

43
Q

what are the 5 charged amino acids and what are their charge?

A

BLAH:
Basic (+)
L: Lysine (k)
A: Arganine (R)
H: Histidine (H)

ADE:
Acidic (-)
D: Aspartic (D)
E: Glutamate (E)

44
Q

What are the 5 polar amino acids?

A

STaNQY

ON
HAP

OH side chains - Serine (Ser,S), theronine, tyrosine
NH2 sde chains - Asparagine (N), glutamine (Q)
Hydroxyl - serine & threonine
Amide - asparagine (N), glutamine (Q)
Phenol - tyrosine (Y)

45
Q

What are the 10 Polar Hydrophobic Amino acids?

A

GLAMP VIP WC

G:Glycine
L: Leucine
A: Alanine
M: Metnionine
P: Phenylalanine

V: Valine
I: Isoleucine
P: Proline
W: Trytophan
C: Cysteine (makes disulphide bonds - SH gr)