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FoM - 1 > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

Features of Protons

A

Positive charge
Mass of +1

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2
Q

Features of Electrons

A

Negative charge
Negligible mass

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3
Q

Features of Neutrons:

A

No charge
Mass of 1

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4
Q

Covelant bond:

A

Formed when unpaired electrons are shared
Strongest type

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5
Q

Ionic bonds

A

Attraction to opposite charges

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6
Q

Hydrogen bonds:

A

Sharing of H atoms

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7
Q

Hydrophobic interaction

A

Interaction of non-polar substances in the presence of polar substances (e.g. water)

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8
Q

Van der waals interaction

A

Interaction of electrons of non-polar substances

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9
Q

Electronegativity:

A

Attractive force that an atomic nucleus exerts on electrons within a bond

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10
Q

Phosphorylation and de-phosphorylation:

A

addition or removal of a phosphoryl group

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11
Q

Acylation reaction:

A

Addition of an acyl group
Relatively stable, useful for joining molecules

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12
Q

Carboxylation

A

Addition of a carboxyl group
Usually occurs at the end of a molecule

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13
Q

What is the end of a molecule referred to as?

A

Reaction centre

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14
Q

Esterification

A

Occurs between acid and alcohol group, producing an ester bond
Water is released

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15
Q

Condensation reaction:

A

Water is removed
Molecules polymerize

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16
Q

Hydrolysis:

A

Water is added, molecules depolymerize

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17
Q

Oxidation-reduction reactions (redox):

A

Electrons transferred from one molecule to another
As one molecule is oxidised, another is reduced

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18
Q

Oxidation and reduction:

A

Oxidation: Loss of electrons
Reduction: Gain of electrons

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19
Q

Oxidation and reduction:

A

Oxidation: Loss of electrons
Reduction: Gain of electrons

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20
Q

Oxidation states of carbon:

A

Vary depending on structure of molecule and electronegativity differences

Charge imbalances help form reactive groups on biological molecules

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21
Q

Monosaccharides:

A

Carbohydrates with a single ring structure

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22
Q

Disaccharides

A

Carbohydrates with a double ring structure

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23
Q

Polysaccharides:

A

Long chains of monosaccharides, storage carbohydrates
E.g. Branching of glycogen enables fast metabolism of glucose

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24
Q

1st law of thermodynamics:

A

Energy is neither created or deystroyed

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25
Q

2nd law of thermodynamics:

A

When energy is converted from one form to another, some of that energy becomes unavailable to do work
No energy transformation is 100% efficient

26
Q

Thermodynamics reactions are reactions involved in change in:

A

Enthalpy (heat content)
Entropy (randomness/disorder)

27
Q

Change in free energy:

A

(energy of products) – (energy of reactants)
𝝙G = 𝝙H - T 𝝙S

28
Q

What does 𝝙G near 0 mean?

A

Reaction is readily reversible

29
Q

Exergonic

A

Total free energy of products is less than total free energy of reactants

Reactions can occur spontaneously

30
Q

Endergonic reactions

A

Total free energy of products is more than total free energy of reactants

Reactions require input of energy

31
Q

Coupling of reactions:

A

Many reactions within the body occur by coupling an unfavorable reaction (positive 𝝙G) with a favorable reaction

e.g. ATP + H2O → ADP + Pi + H+

Therefore, ATP is widely used as energy for many cellular processes

32
Q

Metabolism

A

All reactions taking place in the body

33
Q

Catabolism:

A

Breaking down complex molecules into smaller ones and releasing energy

Yields energy - exergonic and oxidative

34
Q

Anabolism

A

Synthesizing complex molecules out of smaller ones in energy-consuming reactions

Requires energy - endergonic and reductive

35
Q

Polar property of water:

A

Electrons shared unequally causing a difference in change from one side of the molecule to the other

Enables water to act as a universal solvent

36
Q

Shape of water:

A

Tetrahedral
Molecules form a dipole

37
Q

How are water molecules held together?

A

H bonds

38
Q

Hydrophobic effect:

A

When non-polar substances aggregate in aqueous solution and exclude water molecules

E.g. micelles, lipid bilayer, ‘oil slick’

39
Q

Amphipathic molecules:

A

Moelcules with a polar (hydrophilic) ‘head’ and a non-polar (hydrophobic) tail

Form micelles and lipid bilayer of membranes

40
Q

What is a side chain represented by?

A

-R

41
Q

What is an amino group represented by?

A

-NH2

42
Q

Classifications of amino acids:

A
  • Non-polar, hydrophobic
  • Polar, hydrophilic
  • Acidic
  • Basic
43
Q

Peptide bonds:

A

Join amino acids
Produced by condensation reaction
Important for folding proteins

44
Q

What is a base?

A

Proton acceptor

45
Q

What is an acid?

A

Proton donator
Strength depends on how readily it donates proton to base

46
Q

How is acid strength measured?

A

By the acid dissociation constant Ka:
- Ka = [H+][A-]/[HA]
- pKa = -log10[Ka]

47
Q

What is pH and its equation?

A

The measurement of the number of protons in a solution

pH = -log10[H+]

48
Q

What is the Henderson-Hasselbalch equation?

A

Connects the Ka of a weak acid with the pH of a solution containing this acid

pH = pKa + log[A]/[HA]

49
Q

What is a buffer?

A

A solution used to control the pH of a reaction mixture

50
Q

When does pH=pKa?

A

When the concentration of acid is equal to the concentration of the conjugate base

51
Q

Buffer at pKa value…

A

Resist a change in pH on addition of moderate amounts of acid or base

52
Q

How can change in pH affect proteins?

A

Change the ionisation of protein, therefore change its structure and function

53
Q

Primary protein structure:

A

The sequence of amino acid residues

54
Q

Secondary protein structure:

A

Localised conformation of the polypeptide backbone

Hydrogen bonded

55
Q

What are the 3 types of secondary protein structure?

A
  • ⍺ helix
  • β sheet
  • Triple helix
56
Q

Tertiary protein structure:

A

3D structure of entire polypeptide

57
Q

Structure and solubility of tertiary fibrous proteins:

A
  • Mechanically strong e.g. collagen
  • Polypeptide chains are parallel and single axis
  • Insoluble in water
58
Q

Shape and solubility of tertiary globular proteins:

A
  • Spherical e.g. haemoglobin
  • Soluble in water and salt solutions
59
Q

Quaternary protein structure:

A

The spatial arrangement of polypeptide chains in a protein with multiple subunits

E.g. haemoglobin and tropocollagen

60
Q

Haemoglobin structure and function:

A

4 subunits - 2 ⍺ and 2 β chains

Each subunit contains 1 haem group - binds to oxygen

Binding of 1 oxygen changes the affinity of other subunits

61
Q

Tropocollagen structure and function:

A

Structural unit of a collagen fibre

Three helical chains twisted around each other to form a right-handed superhelix

Contains interchain H-bonds and intermolecular covalent bonds

FoM - 1 (40 decks)

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