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zFoM by me > Biochemistry 1-4 πŸ—Έ > Flashcards

Biochemistry 1-4 πŸ—Έ Flashcards

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
Q

polysaccharides

A

long chains of monosaccharides
storage carbohydrates

25
Q

what enables fast metabolism of glucose?

A

branching of glycogen

26
Q

1st law of thermodynamics

A

energy is neither created nor destroyed

27
Q

2nd law of thermodynamics

A

when energy id converted from one form to another, some of that energy is unable to do work

28
Q

enthalpy

A

heat of a reaction

29
Q

entropy

A

measure of disorder

30
Q

where does free energy tend towards after many reactions

A

an unusable state

31
Q

equation for change in free energy

A

𝝙G = 𝝙H - T 𝝙S

32
Q

free energy is related to?

A

the point of equilibrium, if its near 0 it’s reversible

33
Q

Exergonic reations

A

total free energy of products is less than total free energy of reactants
can occur spontaneously

34
Q

Endergonic reactions

A

total free energy of products is more than total free energy of reactants
requires energy input

35
Q

coupling of reactions

A

bodily reactions often occur by coupling an unfavourable reaction with a favourable reaction (ATP is widely used because of this)

36
Q

metabolism

A

all reactions that are taking place in the body

37
Q

Catabolism

A

breaking down complex molecules out of smaller ones and releasing energy

38
Q

Anabolism

A

synthesising complex molecules from smaller molecules, requires energy

39
Q

Properties of water

A

Polar
molecules form a dipole, tetrahedral shape
molecules are held together with H bonding

40
Q

Polar (water)

A

electrons are shared unequally causing a difference in the charge from one side to another
enables water to act as a universal solvent

41
Q

Amphipathic Molecules

A

molecules with polar and nonpolar parts which can form the lipid layer of membranes and micelles

42
Q

Structure of amino acids

A

⍺-carbon is bonded to;
amino group (-NH2)
carboxyl group (-COOH)
hydrogen (-H)
side chain (-R)

43
Q

Classifications of amino acids

A

non-polar
polar
acidic
basic

44
Q

peptide bonds

A

join amino acids
produce condensation reaction
important in folding of proteins

45
Q

Base

A

proton acceptors

46
Q

acid

A

proton donators
strength determined by how readily is donates protons

47
Q

equation for acid dissociation

A

Ka= [H+][A-][HA]
pKa=-log10[Ka]

48
Q

Henderson-Hasselbalch equation

A

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

49
Q

Buffers

A

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
Q

What happens when pH changes in a protein?

A

it can change the ionisation and therefore the structure and function

51
Q

primary protein structure

A

sequence of amino acids

52
Q

Secondary protein structure

A

localised conformation of the poly peptide bond
hydrogen bonded
three tipes:
- ⍺ helix
- Ξ² sheet
- Triple helix

53
Q

Tertiary protein structure

A

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
Q

Quaternary

A

spatial arrangement of polypeptide chains in a protein with multiple subunits

55
Q

Two examples of quateranry

A

haemoglobin or tropocollagen

56
Q

quaternary haemoglobin

A

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
Q

Tropocollagen

A

Structural unit of a collagen fibre
three helical chains twisted around each other to for, a right handed super helix

zFoM by me (37 decks)

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