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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
Coenzyme as prostatic group
Covalently inked w/ enzyme
26
Examples of energy transferring coenzymes and their entities
ATP - phosphate group UDP - monosaccharides CDP - Phosphatidic acids GTP - phosphate group
27
e- and oxygen transferring coenzyme
NADH/N ADPH - e- FMNH2/ FADH2 - e- Porphyrins - e-, oxygen
28
Group transferring coenzymes
CoA - acyl groups Biotin - carboxyl group Lipoid acid - acyl group
29
Types of enzyme inhibition
Irreversible | Reversible
30
Types of reversible inhibition
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
Ki
Inhibitor contant - indicator for how potent an inhibitor is, conc required to produce half maximum inhibition
32
Michaelis-Menten eqn
v = Vmax x [S]/([S] + Km)
33
[S] << Km
v = Vmax x [S]/Km
34
[S] >> Km
v = Vmax
35
[S] = Km
v = Vmax/2
36
[S]
Substrate conc
37
V max
Maximum velocity
38
Class of enzymes
``` Oxidorectases Transferases Hydrolases Lysases Isomerases Ligases ```
39
Oxidoreductases
Oxidation-reduction reactions
40
Examples of oxidoreductases
Dehydrogenases | Oxidase
41
Transferases
Transfer of amino, carboxyl, acyl, methyl, phosphate and other groups between molecules
42
Examples of transferases
Transaminase | Transcarboxylase
43
Hydrolases
Cleavage of bonds coupled w/ inserting water
44
Examples of hydrolases
Esterase Peptidase Amylase
45
Lysases
Cleavage of C-C, C-S and C-N (but not peptide) bonds
46
Examples of lysases
Decarboxylase
47
Isomerases
Rearrangement of bonds
48
Examples of isomerase
Epimerase
49
Ligases
Formation of bonds between C, O S, N
50
Examples of ligases
Synethetase | Carboxylase
51
ALP
Alanine phosphate | Marker of bone disease
52
Creatine Kinase
CK | Marker of muscle damage
53
Regulation of enzyme activity
``` Feedback loops Feedforward activation Allosteric regulation Phosphorylation - dephosphorylation Proteolysis Changes in gene expression ```
54
Feedback loops as a regulator of enzyme activity
Feedback inhibition (product)
55
Feedforward activation as a regulator of enzyme activity
Product activates a downstream enzyme, increasing substrate flow through a pathway
56
Allosteric regulation as a regulator of enzyme activity
Allosteric regulator binds to a site other than the enzyme’s active site, Changes tertiary or quaternary structure
57
Phosphorylation - dephospohorylation as a regulator of enzyme activity
Acts as an on/off switch | Phosphorylation requires kinase and dephosphorylation is performed by phosphatases
58
Proteolysis as a regulator of enzyme activity
Irreversibly activated or inactivated by proteolytic enzymes
59
Changes in gene expression as a regulator of enzyme activity
Increasing or decreasing transcription using transcription factors
60
Stop codons
UAA UAG UGA
61
Alpha helix configuration
Right-handed (clockwise) coiled, 3.6 AA’s per turn
62
Beta-pleated sheets configuration
Polypeptide chain runs in the same direction ---> parallel beta-sheet, polypeptide chain runs in opp direction --> antiparallel beta-sheet
63
Serum protein electrophoresis
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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