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Medicine - year 1 > Into to biochemistry > Flashcards

Into to biochemistry Flashcards

1
Q

When are covalent bonds formed?

A

when unpaired electrons are shared

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2
Q

what is the strongest bond in biomolecules?

A

covalent bonds

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3
Q

what is an ionic bond?

A

attraction of opposite charges

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4
Q

what is a hydrophobic interaction?

A

interaction of non-polar susbstances in the presence of polar substances

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5
Q

what are van der waals interactions?

A

interaction of electrons of non-polar substances

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6
Q

what is electronegativity?

A

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

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7
Q

what is phosphorylation?

A

addition of phosphoryl group

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8
Q

what is dephorphorylation?

A

removal of a phosphoryl group

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9
Q

what is acylation?

A

addition of acyl group

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10
Q

what is carboxylation?

A

addition of a carboxyl group

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11
Q

what is esterification?

A

occurs between acid and alcohol group producing n ester bond

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12
Q

what is released during esterification?

A

water

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13
Q

what is a condensation reaction?

A

where water is removed and molecules are polymerized

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14
Q

what is hydrolysis reaction?

A

water is added and molecules depolymerize

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15
Q

what happens during redox reactions?

A

electrons are transferred from one molecule to another

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16
Q

what is oxidation?

A

loss of electrons

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17
Q

what is reduction?

A

gain of electrons

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18
Q

what are the functions of biomolecules?

A

information storage
structural
energy production
energy storage
carbohydrates
communication

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19
Q

what are the 4 major classes of biomolecules?

A

peptides and proteins
lipids
nucleic acid
carbohydrates

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20
Q

what is glucose called?

A

monosaccharide

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21
Q

what are 2 glucose joined together or glucose joined with fructose called?

A

disaccharide

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22
Q

what is cellulose and glycogen called?

A

polysaccharide

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23
Q

what is the first law of thermodynamics?

A

energy is neither created nor destroyed - total energy before an dafter is the same

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24
Q

what is the second law of thermodynamics?

A

when energy is converted from one form to another, some enegry becomes unavailable to do work - no energy transformation is 100% efficient

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25
Q

in what form is energy released during thermodynamics?

A

carbon dioxide

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26
Q

what happens to the energy released in thermodynamics?

A

becomes disordered

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27
Q

what do thermodynamic reactions involve change in?

A

enthalpy and entropy

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28
Q

what is the formula for aclculating change in free energy?

A

energy of products - energy of reactants

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29
Q

what type of reaction scan occur spontaneously?

A

exergonic reactions

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30
Q

what is an exergonic reaction?

A

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

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31
Q

what is the value of the free energy change in an exergonic reaction?

A

negative

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32
Q

what type of reaction cannot occur spontaneously?

A

endergonic reactions

33
Q

what is an endergonic reaction?

A

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

34
Q

what do endergonic reactions require?

A

the input of energy

35
Q

what is the value of the free energy change in an endergonic reaction?

36
Q

what is the formula for metabolism?

A

catabolism + anabolism

37
Q

what is metabolism?

A

a;; the reactions taking place in the body

38
Q

what is catabolism?

A

the breaking down of larger complex molecules into smaller ones and releasing energy

39
Q

what is anabolism?

A

synthesis of large complex molecules out of smaller ones - energy consuming

40
Q

what is glycolysis?

A

initial breakdown of glucose for generation of ATP

41
Q

what is glucogenesis in the anabolic pathway?

A

the maling of new glucose from non-carbohydrate precursors - costs energy

42
Q

what are 4 properties of water?

A

polar
bent
ion
dipole

43
Q

what type of substances dissolve in water?

A

ionic and polar substances

44
Q

what is water described as being?

A

hydrophilic

45
Q

what does water tend to exclude?

A

hydrocarbons

46
Q

what are hydrocarbons described as being?

A

non-polar and hydrophobic

47
Q

what type of bond dooccurs between hydrogen and a more elevctronegative atom?

A

a polarized bond

48
Q

what is a hydrogen bond?

A

hydrogen interacting with unshared electrons from another electronegative atom

49
Q

what shape do bonds in biomolecules tend to be?

50
Q

what type of molecules are described as being both hydrophilic and hydrophobic?

A

amphipathic molecules

51
Q

what is the structure of amphipathic molecules?

A

polar head at one end and non-polar tail at the other end

52
Q

what do amphipathic molecules form in water?

53
Q

what is an example of a micelle?

A

sodium palmitate

54
Q

what are the 4 classifcations of amino acids?

A

non-polar
polar
acidic
basic

55
Q

what do peptide bonds do?

A

join amino acids

56
Q

what are peptide bonds produced by?

A

condensation reactions

57
Q

what are peptide bonds produced by?

A

condensation reactions

58
Q

what are peptide bonds involved in?

A

the folding of proteins

59
Q

what are some characteristics of peptide bonds?

A

partial double bond
planar
strong and rigid

60
Q

what do acids do?

A

donate proteins

61
Q

wat is the strength of an acid dependent on?

A

how readily is donates a proton

62
Q

what is the strength of an acid measure by?

A

dissociation constant Ka

63
Q

what are bases?

A

proton acceptors

64
Q

what is pH a measurement of?

A

the amount of protons in a solution

65
Q

what is the Henderson-Hasselbalch equation used for?

A

calculating the properties of buffer solutions

66
Q

what is a buffer?

A

a solution used to control pH of a reaction mixture

67
Q

when is pH = pKa?

A

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

68
Q

when is pH = pKa?

A

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

69
Q

what can act as buffers?

70
Q

what can a change in pH cause?

A

change in ionisation which changed its structure and function

71
Q

what is the primary structure of a protein?

A

the sequence of amino acid which forms a polypeptide chain

72
Q

what is the secondary structure of a protein?

A

localised conformation of the polypeptide backbone

73
Q

how is the secondary structure held together?

A

hydrogen bonds

74
Q

what are the 3 types of secondary structures?

A

alpha helix
beta sheet 1 - parallel or anti-paralel
beta sheet 2 - beta pleated sheets

75
Q

what is the tertiary structure?

A

3D structure of entire polypeptide - including all side chains

76
Q

how are tertiary structures stabalised?

A

covalent disulphide bonds
electrostatic interactions
hydrophobic interactions
hydrogen bonds

77
Q

what are 2 examples of tertiary proteins?

A

fibrous proteins and globular proteins

78
Q

how cam protein structures be disrupted/denatured?

A

heat
extremes of pH
detergents
thiol agents and reducing agents

79
Q

what are quarternary structures?

A

spartial arrangement of polypeptide chains in a protein with multiple subunits

Medicine - year 1 (20 decks)

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