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Biochemistry > molecular building blocks of life > Flashcards

molecular building blocks of life Flashcards

(67 cards)

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1
Q

n terminus

A

start of protein molecule

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2
Q

zwitterion

A

core has both positive and negative parts but overall no net charge

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3
Q

asymmetric molecule

A

all 4 sites are different

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4
Q

peptide bond

A

form between amino acids creating a polypeptide chain, rigid as has a partial double bond character
covalent bond
electrons shared between bonded atoms

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5
Q

trans peptide bond

A

oxygen and hydrogen face in opposite directions

1000x more common than cis

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6
Q

cis peptide bond

A

o and h face same direction

1000x less common than trans

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7
Q

chloramphenicol (eye infection treatment)

A

prevents peptide bond formation, binds to ribosome where peptide bonds are made
resistant bacteria use enzyme CAT that stops chloramphenicol from binding to the ribosome

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8
Q

thalidomide

A
  1. good at preventing morning sickness

2. enantiomer causes leg shortness

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9
Q

enantiomer

A

pair of molecules that are a mirror image of each other

2 enantiomers can be formed around the alpha carbon

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10
Q

positively charged amino acids

A

lysine, arginine, histidine

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11
Q

negatively charged amino acids

A

aspartic acid, glutamic acid

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12
Q

carboxylates

A

side chains of negatively charged amino acids

o=c-o-

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13
Q

primary amino groups

A

side chains of positively charged amino acids

n bonded to 2H and 1H+

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14
Q

isomer

A

molecules with the same molecular formula but different arrangements
e.g. D and L form

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15
Q

glycine

A

no D or L form
flexible as small side chain
neurotransmitter

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16
Q

aromatic molecule

A

a molecule that has special properties due to a closed ring of electrons

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17
Q

cysteine

A

thiol group
can bond to other cysteines by a disulphide bond
binds to metals in proteins

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18
Q

disulfide bond

A

covalent bond that forms between side chains of cysteine residues

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19
Q

peptide backbone

A

line of rigid peptide bonds with flexible links that allow folding

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20
Q

carbonyl oxygen

A

slightly negatively charged

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21
Q

amide proton

A

slightly positively charged

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22
Q

alpha helix

A

2nd structure
not made of DNA
peptide bond provides H bonds

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23
Q

prion protein transformation

A

alpha helix is stable but exposed H bonds on beta structure cause sticky velcro ends
single atom changes can cause prion disease

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24
Q

insulin and insulin receptors

A

insulin is a small peptide that acts as a hormone and influences glucose metabolism
transported in the blood, only certain tissues respond
these tissues have insulin specific receptors in their membrane

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25
insulin hexamer
storage molecule of 6 insulin molecules attached found in pancreas injected into diabetics
26
type 1 diabetes
insulin secreting cells destroyed by autoimmune disease
27
kinesins
motor proteins that provide power to move microtubules
28
titin
longest protein known | stops muscles from stretching too far
29
silk beta pleated sheet design
interlocking Ala and Gly residues - rigid spider silk rigid sections alternate with stretchy sections to makethem strong but elastic
30
alpha keratin
stretchy and flexible (hair) unless there are a lot of disulfide bridges (nails)
31
amino acid residue
amino acid once it has become part of a protein - it is a residue of the free amino acid same side chain but its alpha amino and carboxyl groups are now part of peptide bonds
32
myoglobin
subunit of haemoglobin
33
haemoglobin structure
4 units of myoglobin 2 alpha and 2 beta myoglobin binds to haem group that contains an iron ion, which binds to o2 and gives the molecule its red appearance
34
myoglobin saturation
increased sat. at normal tissue conc. | decreased sat. when o2 supply to tissue is low
35
haemoglobin saturation
increased sat. when in lungs | decreased sat. when in tissues
36
sickle cell anaemia
low o2 structure polymerises Hb. | many diseases result from misfolding of proteins, some lead to unwanted polymerisation
37
proteins propagating diseases
beta sheets can stick together | alpha helix is stable but exposed h bonds on beta structure can form sticky velcro ends
38
tamiflu and relenza
anti influenza drugs inhibit neuraminidase neuraminidase removes neuramic acid residues from surface of host cells to ease virus lifecycle
39
penicillin
binds to enzymes that make the bacterial cell wall, stops bacteria from growing
40
Keq
equilibrium constant | ratio of product conc./reactant conc. = Eq
41
gibbs free energy
energy associated with a chemical reaction that can do work
42
transition state/intermediates
intermediate transition states in reactants have higher energy levels than reactants energy is required to generate the intermediate/transition state = activation energy
43
enzyme basic theory
enzymes = biological catalysts enzymes form a complex with the substrate before catalysing its conversion to a product formation of this complex leads to alternative transition state
44
enzyme and Keq
enzymes increase the speed at which Eq is reached, NOT the concentration of products and substrates at Eq
45
catalysis mechanisms
``` proximity orientation strain/distortion, binding puts strain on bond making it easier for reaction to occur acid/base catalysis covalent catalysis ```
46
specificity
only binds to CERTAIN substrates | interaction takes place at active site
47
lock and key model
substrate has a complementary shape to the enzyme active site
48
induced fit model
active site provides strain on the substrate to convert it into the product
49
absolute specificity
the substrate is broken down into 2 absolute molecules
50
bond specificity
the substrate is changed because the enzyme changes a bond within its structure
51
group specificity
a group is added onto the molecule
52
kCat
turnover number | number of substrate molecules that can be converted to product by 1 enzyme in 1 second
53
ways of measuring enzyme activity
substrate disappearance product appearance if coloured using spectrometer
54
km
affinity of enzyme for its substrate stability of enzyme substrate complex high km = low affinity low km = high affinity
55
vmax
fastest rate an enzyme cn catalyse a reaction | only occurs when there is an infinite supply of substrate
56
types of reversible enzyme inhibitors
competitive non competitive uncompetitive
57
types of irreversible enzyme inhibitors
bind by covalent bond bind to a.a. side chain at active site binding permanently inactivates a.s. usually prevents susbtrate binding
58
DFP
sarin nerve gas covalently binds to Ser residue in acetylcholinesterase prevents breakdown of acetylcholine
59
irreversible inhibitors - aspirin
blocks action of prostaglandin H2 synthase by transferring an acetyl group to serine 530
60
penicillin
beta lactam antibiotic covalently binds to Ser residue in penicillin binding protein prevents synthesis of bacterial cell wall peptidoglycan
61
penicillin as an enzyme inhibitor
binds to and irreversibly inhibits bacterial cell wall enzymes covalent bond inhibits cell wall building enzymes
62
bacteria becoming resistant to penicillin
resistant bacteria produces beta latamase | beta lactamase breaks down penicillin
63
augmentin
contains potassium clavulanate which is a beta lactamase irreversible inhibitor
64
competitive inhibitors
competes with substrate for active site often has structure similar to substrate when bound to enzyme prevents binding of substrate can be overcome by increasing substrate until this outcompetes inhibitor
65
non competitive inhibition
``` inhibitor binds away from active site modifies reaction rate still binds substrate with same affinity Km is unaltered vmax decreases ```
66
uncompetitive inhibition
occurs with multisubstrate reactions km decreases vmax decreases binds only to ES complex
67
pH reduces enzyme activity if...
overall 3D structure of a.s. is altered | group involved in substrate binding or catalytic event changes charge

Biochemistry (8 decks)

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