Biochemistry 1-4 πŸ—Έ Flashcards

(58 cards)

1
Q

proton

A

positive charge
mass of +1

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1
Q

electrons

A

negative charge
negligible mass

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2
Q

neutrons

A

no charge
mass of 1

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3
Q

Covalent bonding

A

formed when unpaired electrons are shared
strongest type of bond

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4
Q

hydrogen bond

A

the sharing of H atoms

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5
Q

ionic bond

A

attraction of opposite charges

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6
Q

hydrophobic interaction

A

interaction of non-polar substances in the presence of polar substances (especially water)

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7
Q

van der waals interaction

A

interaction of electrons of non-polar substances

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8
Q

electronegativity

A

the attractive force that an atomic nucleus exerts on electrons within a bond

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9
Q

phosphorylation/dephosphorylation

A

the adding/taking away of a phosphoryl group

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10
Q

acylation

A

addition of an acyl group

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11
Q

features of an acyl group

A

relatively stable
useful for joining molecules

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12
Q

carboxylation

A

the addition of a carboxyl group

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13
Q

where do carboxyl groups bind?

A

usually the end of molecules (reactive centre)

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14
Q

esterification

A

occurs between acid and alcohol group, producing an ester bond.
water will be 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

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18
Q

oxidation

A

is loss of electrons

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19
Q

reduction

A

is gain of electrons

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20
Q

What are the oxidation states of carbon?

A

vary depending on structure of the molecule and electronegativity differences

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21
Q

what do the charge imbalances of carbon help with?

A

forming reactive groups on biological molecules

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22
Q

monosaccharide

A

carbohydrates with a single ring structure

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23
Q

disaccharides

A

carbohydrates with double ring structure

24
polysaccharides
long chains of monosaccharides storage carbohydrates
25
what enables fast metabolism of glucose?
branching of glycogen
26
1st law of thermodynamics
energy is neither created nor destroyed
27
2nd law of thermodynamics
when energy id converted from one form to another, some of that energy is unable to do work
28
enthalpy
heat of a reaction
29
entropy
measure of disorder
30
where does free energy tend towards after many reactions
an unusable state
31
equation for change in free energy
𝝙G = 𝝙H - T 𝝙S
32
free energy is related to?
the point of equilibrium, if its near 0 it’s reversible
33
Exergonic reations
total free energy of products is less than total free energy of reactants can occur spontaneously
34
Endergonic reactions
total free energy of products is more than total free energy of reactants requires energy input
35
coupling of reactions
bodily reactions often occur by coupling an unfavourable reaction with a favourable reaction (ATP is widely used because of this)
36
metabolism
all reactions that are taking place in the body
37
Catabolism
breaking down complex molecules out of smaller ones and releasing energy
38
Anabolism
synthesising complex molecules from smaller molecules, requires energy
39
Properties of water
Polar molecules form a dipole, tetrahedral shape molecules are held together with H bonding
40
Polar (water)
electrons are shared unequally causing a difference in the charge from one side to another enables water to act as a universal solvent
41
Amphipathic Molecules
molecules with polar and nonpolar parts which can form the lipid layer of membranes and micelles
42
Structure of amino acids
⍺-carbon is bonded to; amino group (-NH2) carboxyl group (-COOH) hydrogen (-H) side chain (-R)
43
Classifications of amino acids
non-polar polar acidic basic
44
peptide bonds
join amino acids produce condensation reaction important in folding of proteins
45
Base
proton acceptors
46
acid
proton donators strength determined by how readily is donates protons
47
equation for acid dissociation
Ka= [H+][A-]\[HA] pKa=-log10[Ka]
48
Henderson-Hasselbalch equation
pH=pKa+log[A]/[HA]
49
Buffers
a solution used to control the pH of a reaction mixture that resists a change in pH when moderate amounts of acid or base are added when the acid concentration is equal to the conjugate base (pH=pKa)
50
What happens when pH changes in a protein?
it can change the ionisation and therefore the structure and function
51
primary protein structure
sequence of amino acids
52
Secondary protein structure
localised conformation of the poly peptide bond hydrogen bonded three tipes: - ⍺ helix - β sheet - Triple helix
53
Tertiary protein structure
3D structure of an entire polypeptide fibrous: mechanically strong, insoluble in water, the chains are parallel globular: spherical, soluble in water and salt solutions
54
Quaternary
spatial arrangement of polypeptide chains in a protein with multiple subunits
55
Two examples of quateranry
haemoglobin or tropocollagen
56
quaternary haemoglobin
4 subunits, 2 alpha & 2 beta each subunit has on haem group which binds to oxygen each oxygen binding changes the affinity of other subunits
57
Tropocollagen
Structural unit of a collagen fibre three helical chains twisted around each other to for, a right handed super helix