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MBBS - Year 1 > Biochem - Infection and Immunity > Flashcards

Biochem - Infection and Immunity Flashcards

1
Q

Acidic functional groups of AA

A

Carboxyl

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2
Q

Basic functional groups of AA

A

Amine
Imidazole
Guanidino

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3
Q

Neutral functional groups of AA

A

Glycine
Amides
Hydroxyl
Sulfhydryl -SH

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4
Q

Aliphatic functional groups of AA

A

Hydrocarbon

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5
Q

Aromatic functional groups of AA

A

Carbon rings

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6
Q

Start codon

A

Met is coded for by AUG - signifies start of chain

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7
Q

When is rotation of adjacent peptides allowed

A

At N-C (central)

C (central) -C

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8
Q

Structure of proteins

A

Linear, unbranched

heteropolymers

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9
Q

Size of proteins

A

50 to >2,000 AA

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10
Q

Primary structure of proteins

A

Order of AA = sequence

Always written from amino end to carboxyl e.g NH2 - His- Leu-Thr- Pro -COOH

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11
Q

Alpha helix

A

Rod like structure: polypeptide chain tightly coiled, amino acid side chains extending outwards from the helix axis
Stabilised by H-bonds: backbone amine (NH) and carbonyl (CO) group, 4 residues away along the chain

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12
Q

Beta pleated sheet

A

Zigzag structure: C-C bonds are tetrahedral –> cannot exist in planar configuration
Stabilised by H bonds: backbone amide (NH) and carboxyl (CO) groups, between diff parts of the chain or between diff chains

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13
Q

Types of proteins

A

Globular
Fibrous
Soluble
Membrane

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14
Q

Globular proteins

A

Compact spheres (haemoglobin, albumin)

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15
Q

Fibrous proteins

A

Filamentous molecules (collagen, keratin)

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16
Q

Soluble proteins

A

Dissolve in water (Hb, immunoglobulins)

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17
Q

Membrane proteins

A

Associated w/ membranes (glucose transporter)

Integral protein with a single transmembrane helix
Integral protein w/ multiple transmembrane helix
Peripheral proteins w/ lipid anchors
Peripheral proteins attached to the membrane

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18
Q

Biological function of enzymes

A 
Part of metabolic pathways (glycolysis)
Signal transduction and cell regulation (kinases, phosphatases)
Digestion (amylases, proteases)
Movement (myosin)
Energy production (ATP synthase)
Drug metabolism (monooxygenases)
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19
Q

Principles of enzyme catalysis

A

Enzymes are catalysts
Enzymes cannot alter the equilibrium of a reaction
Enzymes accelerate chemical reactions

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20
Q

Km

A

Measure for the stability of the esc

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21
Q

Large Km (~ 10^-3M)

A

Low substrate enzyme eaffibty

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22
Q

Small Km (~10^-5M)

A

High substrate-enzyme affinity

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23
Q

Coenzymes

A

Helper molecules that play a big part in enzyme-catalysed reactions

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24
Q

Coenzyme as co-substrate

A

Reversibly bound to enzyme

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25
Q

Coenzyme as prostatic group

A

Covalently inked w/ enzyme

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26
Q

Examples of energy transferring coenzymes and their entities

A

ATP - phosphate group
UDP - monosaccharides
CDP - Phosphatidic acids
GTP - phosphate group

27
Q

e- and oxygen transferring coenzyme

A

NADH/N ADPH - e-
FMNH2/ FADH2 - e-
Porphyrins - e-, oxygen

28
Q

Group transferring coenzymes

A

CoA - acyl groups
Biotin - carboxyl group
Lipoid acid - acyl group

29
Q

Types of enzyme inhibition

A

Irreversible

Reversible

30
Q

Types of reversible inhibition

A

Comp - enzyme can bind substrate or competitive inhibitor, but not both at same time
Non - comp - enzyme or esc can bind non-competitive inhibitor, and also create enzyme-substrate-inhibitor complex

31
Q

Ki

A

Inhibitor contant - indicator for how potent an inhibitor is, conc required to produce half maximum inhibition

32
Q

Michaelis-Menten eqn

A

v = Vmax x [S]/([S] + Km)

33
Q

[S] &laquo_space;Km

A

v = Vmax x [S]/Km

34
Q

[S]&raquo_space; Km

A

v = Vmax

35
Q

[S] = Km

A

v = Vmax/2

36
Q

[S]

A

Substrate conc

37
Q

V max

A

Maximum velocity

38
Q

Class of enzymes

A 
Oxidorectases 
Transferases 
Hydrolases 
Lysases 
Isomerases 
Ligases
39
Q

Oxidoreductases

A

Oxidation-reduction reactions

40
Q

Examples of oxidoreductases

A

Dehydrogenases

Oxidase

41
Q

Transferases

A

Transfer of amino, carboxyl, acyl, methyl, phosphate and other groups between molecules

42
Q

Examples of transferases

A

Transaminase

Transcarboxylase

43
Q

Hydrolases

A

Cleavage of bonds coupled w/ inserting water

44
Q

Examples of hydrolases

A

Esterase
Peptidase
Amylase

45
Q

Lysases

A

Cleavage of C-C, C-S and C-N (but not peptide) bonds

46
Q

Examples of lysases

A

Decarboxylase

47
Q

Isomerases

A

Rearrangement of bonds

48
Q

Examples of isomerase

A

Epimerase

49
Q

Ligases

A

Formation of bonds between C, O S, N

50
Q

Examples of ligases

A

Synethetase

Carboxylase

51
Q

ALP

A

Alanine phosphate

Marker of bone disease

52
Q

Creatine Kinase

A

CK

Marker of muscle damage

53
Q

Regulation of enzyme activity

A 
Feedback loops 
Feedforward activation 
Allosteric regulation 
Phosphorylation - dephosphorylation 
Proteolysis 
Changes in gene expression
54
Q

Feedback loops as a regulator of enzyme activity

A

Feedback inhibition (product)

55
Q

Feedforward activation as a regulator of enzyme activity

A

Product activates a downstream enzyme, increasing substrate flow through a pathway

56
Q

Allosteric regulation as a regulator of enzyme activity

A

Allosteric regulator binds to a site other than the enzyme’s active site, Changes tertiary or quaternary structure

57
Q

Phosphorylation - dephospohorylation as a regulator of enzyme activity

A

Acts as an on/off switch

Phosphorylation requires kinase and dephosphorylation is performed by phosphatases

58
Q

Proteolysis as a regulator of enzyme activity

A

Irreversibly activated or inactivated by proteolytic enzymes

59
Q

Changes in gene expression as a regulator of enzyme activity

A

Increasing or decreasing transcription using transcription factors

60
Q

Stop codons

A

UAA
UAG
UGA

61
Q

Alpha helix configuration

A

Right-handed (clockwise) coiled, 3.6 AA’s per turn

62
Q

Beta-pleated sheets configuration

A

Polypeptide chain runs in the same direction —> parallel beta-sheet, polypeptide chain runs in opp direction –> antiparallel beta-sheet

63
Q

Serum protein electrophoresis

A

Lab test analysing proteins in blood
Serum proteins separated by their size and charge
Albumin is lightest and Ig’s are heaviest

MBBS - Year 1 (93 decks)

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