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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
2nd law of thermodynamics:
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
Thermodynamics reactions are reactions involved in change in:
Enthalpy (heat content) Entropy (randomness/disorder)
27
Change in free energy:
(energy of products) – (energy of reactants) 𝝙G = 𝝙H - T 𝝙S
28
What does 𝝙G near 0 mean?
Reaction is readily reversible
29
Exergonic
Total free energy of products is less than total free energy of reactants Reactions can occur spontaneously
30
Endergonic reactions
Total free energy of products is more than total free energy of reactants Reactions require input of energy
31
Coupling of reactions:
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
Metabolism
All reactions taking place in the body
33
Catabolism:
Breaking down complex molecules into smaller ones and releasing energy Yields energy - exergonic and oxidative
34
Anabolism
Synthesizing complex molecules out of smaller ones in energy-consuming reactions Requires energy - endergonic and reductive
35
Polar property of water:
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
Shape of water:
Tetrahedral Molecules form a dipole
37
How are water molecules held together?
H bonds
38
Hydrophobic effect:
When non-polar substances aggregate in aqueous solution and exclude water molecules E.g. micelles, lipid bilayer, ‘oil slick’
39
Amphipathic molecules:
Moelcules with a polar (hydrophilic) ‘head’ and a non-polar (hydrophobic) tail Form micelles and lipid bilayer of membranes
40
What is a side chain represented by?
-R
41
What is an amino group represented by?
-NH2
42
Classifications of amino acids:
- Non-polar, hydrophobic - Polar, hydrophilic - Acidic - Basic
43
Peptide bonds:
Join amino acids Produced by condensation reaction Important for folding proteins
44
What is a base?
Proton acceptor
45
What is an acid?
Proton donator Strength depends on how readily it donates proton to base
46
How is acid strength measured?
By the acid dissociation constant Ka: - Ka = [H+][A-]/[HA] - pKa = -log10[Ka]
47
What is pH and its equation?
The measurement of the number of protons in a solution pH = -log10[H+]
48
What is the Henderson-Hasselbalch equation?
Connects the Ka of a weak acid with the pH of a solution containing this acid pH = pKa + log[A]/[HA]
49
What is a buffer?
A solution used to control the pH of a reaction mixture
50
When does pH=pKa?
When the concentration of acid is equal to the concentration of the conjugate base
51
Buffer at pKa value…
Resist a change in pH on addition of moderate amounts of acid or base
52
How can change in pH affect proteins?
Change the ionisation of protein, therefore change its structure and function
53
Primary protein structure:
The sequence of amino acid residues
54
Secondary protein structure:
Localised conformation of the polypeptide backbone Hydrogen bonded
55
What are the 3 types of secondary protein structure?
- ⍺ helix - β sheet - Triple helix
56
Tertiary protein structure:
3D structure of entire polypeptide
57
Structure and solubility of tertiary fibrous proteins:
- Mechanically strong e.g. collagen - Polypeptide chains are parallel and single axis - Insoluble in water
58
Shape and solubility of tertiary globular proteins:
- Spherical e.g. haemoglobin - Soluble in water and salt solutions
59
Quaternary protein structure:
The spatial arrangement of polypeptide chains in a protein with multiple subunits E.g. haemoglobin and tropocollagen
60
Haemoglobin structure and function:
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
Tropocollagen structure and function:
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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