Biochemistry

?
what is the mutation that leads to sickle cell?
healthy glutamate is replaced with unhealthy valine
1 of 60
what happens to the red blood cells in someone with sickle cell?
they become rigid and shaped like a crescent because hemoglobin inside them clumps up. they stick to vessel walls causing a block.
2 of 60
what are the two types of macromolecules, give examples.
informational eg DNA, structural eg cellulose.
3 of 60
what happens to monosaccharides with more than 3 carbons in water?
the atoms bend to form ring structures.
4 of 60
what is the structure of myosin?
fibrous alpha helical chain, globular head group.
5 of 60
what can hydrogen bonding lead to?
can compete with structural/functional interactions in biomolecules which compels proteins to adopt contorted shapes
6 of 60
what amino acids often occur in collagen?
glycine and proline
7 of 60
what does scurvy result from?
lack of vitamin C which is needed to make collagen. different types of tissues break down.
8 of 60
why aren't disulfide bridges found inside our cells?
because of the reducing conditions in our cells.
9 of 60
which enzymes occur widely in active sites?
serine and aspartate
10 of 60
which enzymes are good for binding calcium?
glutamate and aspartate
11 of 60
which amino acids undergo phosphorylation?
serine, threonine, tyrosine
12 of 60
which amino acids undergo glycosylation?
serine, threonine, asparagine
13 of 60
what is pKa?
the pH at which a weakly acidic group is 50% dissociated.
14 of 60
Describe right handed alpha helix.
Each CO is hydrogen bonded to the amino residue. 3.6 residues every turn. interrupted by loops.
15 of 60
Describe beta pleated sheets.
multiple B strands side by side. parallel and antiparallel sheets. hydrogen bonding between adjacent strands.
16 of 60
What are motifs?
recurring geometric combinations of secondary structure
17 of 60
describe the features of myoglobin
globular, contains heme, 75% alpha helical, compact
18 of 60
what are domains?
independently folded, compact units in proteins, 25 to 300 amino acid residues long
19 of 60
Describe the features of HbA.
An alpha globin, beta globin tetramer. Its subunits are organised into pairs of dimers. Tertiary structure is largely alpha helical (no beta sheet or disulfide bridges) and each subuint has a heme group.
20 of 60
Describe the structure of collagen.
extracellular protein. Tropocollagen molecule. 3 left-handed chains coiled around each other in a right-handed supercoil. consists of staggered alignments of tropocollagens covalently cross linked by aldol links.
21 of 60
how does an enzyme work?
it orientates the substrates, reducing the activation energy, stabilising the transition state.
22 of 60
what things can happen if a solution is exposed to ER?
photoluminescence, transmission, scattering
23 of 60
Explain how lactate dehydrogenase works to form lactate.
Pyruvate binds to arginine 171. arginine 109 closes the lid and strains the CO bond, stabilising transition state. NADH donates a hydride becoming NAD+. Histidine 195 donates a proton.
24 of 60
explain an experiment in which colorimetry can be used
b-lactamase degrades penicillin. can use a modified form of penicillin
25 of 60
what does AchE do?
degrade the neurotransmitter acetyl choline allowing repeated firing of neurones.
26 of 60
Name the things that feed the TCA cycle
fatty acids, proteins, fats, carbohydrates
27 of 60
what hormones maintain catabolic reactions?
glucogen and adrenaline
28 of 60
what does catabolism make?
ATP and NADH
29 of 60
which coenzyme is used in anabolic reactions?
NADP+
30 of 60
which stages of glycolysis use atp?
1 and 3
31 of 60
which stages form atp?
7 and 10
32 of 60
what is the perfect enzyme?
triose phosphate isomerase
33 of 60
name all the enzymes used in glycolysis
hexokinase, glucose-6-phosphate isomerase, phosphofructokinase, aldolase, triose phosphate isomerase, glyceraldehyde dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, enolase, pyruvate kinase
34 of 60
what does 23BPG do?
interacts with hemoglobin and acts as a metabolic flag showing we need oxygen to break it down to its waste products. hemoglobin is pushed into its T state where it releases heme and allows for oxygen to be released
35 of 60
what enzyme forms lactate from pyruvate and what else does it form?
lactate dehydrogenase, NAD+
36 of 60
how is ethanol formed from pyruvate?
pyruvate decarboxylase converts it to acetaldehyde and alcohol dehydrogenase converts that to ethanol.
37 of 60
Name the enzymes used in gluconeogenesis
pyruvate carboxylase, PEPCK, fructose-1,6-bisphosphatase, glucose-6-phosphatase.
38 of 60
how many ATPs does gluconeogenesis use?
4
39 of 60
what does the TCA cycle form?
3 NADHs, 1 SH-CoA, 2 CO2s, 1 QH2, 1 GTP
40 of 60
where does glycolysis occur?
skeletal muscle
41 of 60
give four energy uses of ATP?
active transport, dna replication, luminescence, metabolism
42 of 60
explain the process of creating a proton gradient
Electrons start at complex I which can move 4 protons through it. FMN transfers them to complex III. CoQ diffuses to I, takes the electrons from fe-s, becoming CoQH2, moving 2 protons across. diffuses to III, 2 protons pumped through.
43 of 60
Name and describe the parts of ATP synthase
bit in the membrane- Fo, Y attaches from it into the catalytic part made of alpha and beta. stalk attached to it by d.
44 of 60
what is Fo inhibited by?
oligomycin
45 of 60
how is metabolism regulated?
transcription, protein degradation, change in activity of enzyme
46 of 60
what is feedforward activation?
when the concentration of a metabolite has an activation effect on an enzyme within a biosynthetic pathway
47 of 60
what are the intermediates signalling glycolysis is unnecessary?
High citrate, high acetyl CoA, high ATP, low AMP
48 of 60
what is phosphofructokinase inhibited by?
ATP, PEP, citrate
49 of 60
what amino acids can act as hydrogen donors?
arg, lys, trp
50 of 60
what amino acids can act as hydrogen acceptors?
asp, glu
51 of 60
what amino acids can act as hydrogen donors and acceptors?
arn, gln, ser, thr, tyr
52 of 60
how many reactions does fatty cid oxidation last?
3
53 of 60
what is an amphibolic cycle?
involves anabolism and catabolism
54 of 60
what are anaplerotic reactions?
form intermediates in a metabolic pathway
55 of 60
what does G6P inhibit in glycolysis?
hexokinase
56 of 60
what activates pyruvate kinase in glycolysis?
F16BP
57 of 60
what des aceytl CoA do in gluconeogenesis?
activates pyruvate carboxylase
58 of 60
in bacteria, what does PEP inhibit?
PFK
59 of 60
What inhibits the TCA cycle?
NADH
60 of 60

Other cards in this set

Card 2

Front

what happens to the red blood cells in someone with sickle cell?

Back

they become rigid and shaped like a crescent because hemoglobin inside them clumps up. they stick to vessel walls causing a block.

Card 3

Front

what are the two types of macromolecules, give examples.

Back

Preview of the front of card 3

Card 4

Front

what happens to monosaccharides with more than 3 carbons in water?

Back

Preview of the front of card 4

Card 5

Front

what is the structure of myosin?

Back

Preview of the front of card 5
View more cards

Comments

No comments have yet been made

Similar Biology resources:

See all Biology resources »See all biochemistry resources »