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Medicine - year 1 > Into to biochemistry > Flashcards

Into to biochemistry Flashcards

(79 cards)

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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
in what form is energy released during thermodynamics?
carbon dioxide
26
what happens to the energy released in thermodynamics?
becomes disordered
27
what do thermodynamic reactions involve change in?
enthalpy and entropy
28
what is the formula for aclculating change in free energy?
energy of products - energy of reactants
29
what type of reaction scan occur spontaneously?
exergonic reactions
30
what is an exergonic reaction?
total free energy of products is less than total free energy of reactants
31
what is the value of the free energy change in an exergonic reaction?
negative
32
what type of reaction cannot occur spontaneously?
endergonic reactions
33
what is an endergonic reaction?
total free energy of products is more than the total free energy of reactants
34
what do endergonic reactions require?
the input of energy
35
what is the value of the free energy change in an endergonic reaction?
positive
36
what is the formula for metabolism?
catabolism + anabolism
37
what is metabolism?
a;; the reactions taking place in the body
38
what is catabolism?
the breaking down of larger complex molecules into smaller ones and releasing energy
39
what is anabolism?
synthesis of large complex molecules out of smaller ones - energy consuming
40
what is glycolysis?
initial breakdown of glucose for generation of ATP
41
what is glucogenesis in the anabolic pathway?
the maling of new glucose from non-carbohydrate precursors - costs energy
42
what are 4 properties of water?
polar bent ion dipole
43
what type of substances dissolve in water?
ionic and polar substances
44
what is water described as being?
hydrophilic
45
what does water tend to exclude?
hydrocarbons
46
what are hydrocarbons described as being?
non-polar and hydrophobic
47
what type of bond dooccurs between hydrogen and a more elevctronegative atom?
a polarized bond
48
what is a hydrogen bond?
hydrogen interacting with unshared electrons from another electronegative atom
49
what shape do bonds in biomolecules tend to be?
linear
50
what type of molecules are described as being both hydrophilic and hydrophobic?
amphipathic molecules
51
what is the structure of amphipathic molecules?
polar head at one end and non-polar tail at the other end
52
what do amphipathic molecules form in water?
micelles
53
what is an example of a micelle?
sodium palmitate
54
what are the 4 classifcations of amino acids?
non-polar polar acidic basic
55
what do peptide bonds do?
join amino acids
56
what are peptide bonds produced by?
condensation reactions
57
what are peptide bonds produced by?
condensation reactions
58
what are peptide bonds involved in?
the folding of proteins
59
what are some characteristics of peptide bonds?
partial double bond planar strong and rigid
60
what do acids do?
donate proteins
61
wat is the strength of an acid dependent on?
how readily is donates a proton
62
what is the strength of an acid measure by?
dissociation constant Ka
63
what are bases?
proton acceptors
64
what is pH a measurement of?
the amount of protons in a solution
65
what is the Henderson-Hasselbalch equation used for?
calculating the properties of buffer solutions
66
what is a buffer?
a solution used to control pH of a reaction mixture
67
when is pH = pKa?
when the concentration of acid is equal to the concentration of the conjugate base
68
when is pH = pKa?
when the concentration of acid is equal to the concentration of the conjugate base
69
what can act as buffers?
proteins
70
what can a change in pH cause?
change in ionisation which changed its structure and function
71
what is the primary structure of a protein?
the sequence of amino acid which forms a polypeptide chain
72
what is the secondary structure of a protein?
localised conformation of the polypeptide backbone
73
how is the secondary structure held together?
hydrogen bonds
74
what are the 3 types of secondary structures?
alpha helix beta sheet 1 - parallel or anti-paralel beta sheet 2 - beta pleated sheets
75
what is the tertiary structure?
3D structure of entire polypeptide - including all side chains
76
how are tertiary structures stabalised?
covalent disulphide bonds electrostatic interactions hydrophobic interactions hydrogen bonds
77
what are 2 examples of tertiary proteins?
fibrous proteins and globular proteins
78
how cam protein structures be disrupted/denatured?
heat extremes of pH detergents thiol agents and reducing agents
79
what are quarternary structures?
spartial arrangement of polypeptide chains in a protein with multiple subunits

Medicine - year 1 (20 decks)

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