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KAPS Paper 1 > CHEMISTRY > Flashcards

CHEMISTRY Flashcards

1
Q

DICARBOXYLIC ACIDS

A

OH MY SUCH GOOD APPLE PIE, SWEET AS SUGAR:

Oxalic acid (HOOC-COOH)
Malonic acid (HOOC-CH2-COOH)
Succinic acid (HOOC-CH2-CH2-COOH)
Glutaric acid (HOOC-(CH2)3-COOH)
Adipic acid (HOOC-(CH2)4-COOH)
Pimelic acid (HOOC-(CH2)5-COOH)
Suberic acid (HOOC-(CH2)6-COOH)
Azelaic acid (HOOC-(CH2)7-COOH)
Sebacic acid (HOOC-(CH2)8-COOH)

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2
Q

monocarboxylic acids

A

THE FLIGHT ATTENDANT OF THE PLANE BUY A VALERIAN CAP TO ENTERTAIN CAPRIL AND PELARGO

Formic acid (HCOOH)
Acetic acid (CH3COOH)
Propionic acid (CH3CH2COOH)
Butyric acid (CH3CH2CH2COOH)
Valeric acid (CH3(CH2)3COOH)
Caproic acid (CH3(CH2)4COOH)
Enanthic acid (CH3(CH2)5COOH)
Caprylic acid (CH3(CH2)6COOH)
Pelargonic acid (CH3(CH2)7COOH)

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3
Q

ARRANGEMENT ACCORDING TO ACIDITY

A

ELEMENT
most electronegative
BCNOF flourine most
heaviest
FClBrI Iodine most

RESONANCE- aromatic rings

CONDUCTIVITY- no of electronegative atoms

HYBRIDIZATION- sp or triple bond most acidic

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4
Q

Type of prodrugs

A

1.carrier
2.bioprecursor

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5
Q

Type of carrier prodrugs

A
  1. Bipartite
  2. Tripartite
  3. Codrugs
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6
Q

Activation of carrier prodrug is cause by which reaction

A

Hydrolysis

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7
Q

Activation of bioprecursor prodrugs is cause by?

A

Redox

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8
Q

Chemical groups having similar physicochemical properties
Which give similar biological effects

A

Bioisosteres

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9
Q

Phase 1 metebolism reactions:

A

HORD

Hydrolysis
Oxidation- CYP450
Reduction
Deamination

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10
Q

In phase 2 glucoronidation metabolism, which enzyme facilitates the reaction?

A

UDP glucoronosyl transferase

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11
Q

Metabolic pathway/conjugation present in neonates/ infants (Sanggol)

A

Sulfate conjugation

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12
Q

Paracetamol is metabolized by which conjugation process?

A

Glutathione Conjugation

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13
Q

Carbohydrates contains which functional groups

A

Carbonyl group:
Ketones R-C=O-R
Aldehydes R-C=O-H

+Polyalcohols -OH

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14
Q

Suffix of monosaccharides containing ketone group

A

-ulose

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15
Q

Disacharide MALTOSE composition

A

2 glucose

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16
Q

Disacharide LACTOSE composition

A

Gluc/galactose

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17
Q

Disacharide SUCROSE composition

A

Gluc/Fructose

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18
Q

Trisaccharide RAFFINOSE composition

A

Gluc/fruc/galactose

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19
Q

Tetrasaccharide STACHYOSE composition

A

Gluc/fruc/ 2-galactose

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20
Q

Metabolic process which converts GLUCOSE into PYRUVATE

A

GLYCOLYSIS

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21
Q

10 steps of glycolisis

A

Great grandmother throws fresh fruit dish & go by picking pumpkins to prepare pies
1. Glucose phosphorylation
2. Isomerization of glucose-6-phosphate
3. Second phosphorylation
4. Cleavage of fructose-1,6-bisphosphate
5. Isomerization of dihydroxyacetone phosphate
6. Phosphorylation of 3-phosphoglycerate
7. Conversion of 3-phosphoglycerate to 2-phosphoglycerate
8. Enolase-mediated dehydration
9. Phosphorylation of 2-phosphoglycerate
10. Substrate-level phosphorylation to generate pyruvate

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22
Q

Meaning of Mnemonics DGB
In great grandma throws fresh fruits DISH & GO BY picking pumpkins to prepare pies
-10 steps of glycolysis

A

DihydroxyAcetone Phosphate
GlycerAldehyde 3-Phosphate
1,3- BiphosphoGlycerate

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23
Q

Enzymes involved in glycolysis metabolism

A

He Put the Phone And Tried to Get the Plastic Plate to Eat Pie

Hexokinase
PhosphoFructo Isomerase
PhosphoFructoKinase
Aldolase
Trios Phosphate Isomerase
Glyceraldehyde 3-Phosphate Dehydrogenase
PhosphoGlyceroKinase
PhosphoGlyceroMutase
Enolase
Pyruvate Kinase

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24
Q

No. Of ATP yeilded from GLYCOLYSIS

A

5 or 7

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25
Q

End product of ANAEROBIC glycolysis in vertebrates

A

L-lactate
Total ATP yield = 2

By enzyme LACTATE DEHYDROGENASE

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26
Q

End product of ANAEROBIC glycolysis in microorganisms

A

Ethanol

By enzyme- PYRUVATE DECARBOXYLASE

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27
Q

Gluconeogenesis will covert pyruvate to oxaloacetate- G6P by the enzyme

A

PYRUVATE CARBOXYLASE

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28
Q

End product of AEROBIC glycolysis

A

Acetyl-CoA

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29
Q

Major pathway for formation of ATP. Also provides substrate for gluconeogenesis, AA & FA synthesis

A

TCA/ CITRIC ACID/ KREB’s cycle
Occuring in mitochondria

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30
Q

End products of KREB’s CYCLE

A

2 CO2
1 GTP
3 NADH
1 FADH2

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31
Q

RLS (rate limiting step) of KREB’s CYCLE

A

Conversion of
Isocitrate to
alpha-ketoglutarate

By enzyme isocitrate dehydrogenase

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32
Q

RLS (rate limiting step) of glycolysis

A

conversion of
fructose-6-phosphate
to fructose-1,6-bisphosphate

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33
Q

4 fates of PYRUVATE

A

Ethanol- microorganisms ANAErobic
Lactate- vertebrates ANAErobic
G6P- gluconeogenis
Acetyl-CoA- AEROBIC

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34
Q

Substrates (steps) of Kreb’s cycle/citric Ac/ TCA

A

On Campus Areas, I Kiss Sexy Seductive Fair Maidens

Oxaloacetate
Citrate
Aconitate
Isocitrate
α-Ketoglutarate
Succinyl-CoA
Succinate
Fumarate
Malate

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35
Q

Total ATP yeild from TCA

A

10 ATP

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36
Q

Total ATP yeild of complete glucose oxidation

A

30/32 ATP

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37
Q

The substrates for gluconeogenesis, which is the process of synthesizing glucose from non-carbohydrate precursors, include:

A
  1. Pyruvate
  2. Lactate
  3. Glycerol (from triglycerides)
  4. Glucogenic amino acids (amino acids that can be converted to intermediates of the Kreb cycle)

Reverse of glycolysis

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38
Q

A metabolic pathway in which lactate produced by anaerobic glycolysis in muscles is transported to the liver and converted back to glucose.

A

CORI CYCLE

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39
Q
  1. GSD Type I (Von Gierke Disease):
    • Defective Enzyme:
A

Glucose-6-phosphatase

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40
Q
  1. GSD Type II (Pompe Disease):
    • Defective Enzyme:
A

Acid alpha-glucosidase (GAA)

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41
Q
  1. GSD Type III (Cori Disease):
    • Defective Enzyme:
A

Glycogen debranching enzyme (Amylo-1,6-glucosidase)

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42
Q
  1. GSD Type IV (Andersen Disease):
    • Defective Enzyme:
A

Glycogen branching enzyme (GBE1)

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43
Q
  1. GSD Type V (McArdle Disease):
    • Defective Enzyme:
A

Muscle glycogen phosphorylase

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44
Q
  1. GSD Type VI (Hers Disease):
    • Defective Enzyme:
A

Liver glycogen phosphorylase

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45
Q
  1. GSD Type IX:
    • Various subtypes with defects in different enzymes like
A

phosphorylase kinase, phosphoglucomutase, and others depending on the subtype.

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46
Q

Glycogen storage diseases (GSDs)

A

VPCAMHT
Viagra Pills Cause A Major Hard Turnon

1.	GSD Type I: Von Gierke Disease
2.	GSD Type II: Pompe Disease
3.	GSD Type III: Cori Disease
4.	GSD Type IV: Andersen Disease
5.	GSD Type V: McArdle Disease
6.	GSD Type VI: Hers Disease
7.	GSD Type VII: Tarui
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47
Q

The biochemical process through which glycogen, a polysaccharide composed of glucose units, is broken down into glucose molecules

A

Glycogenolysis

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48
Q

also known as the pentose phosphate pathway (PPP) or phosphogluconate pathway, is a series of biochemical reactions that occur in the cytoplasm of cells.

A

Hexose Monophosphate (HMP) shunt
G6PD- RLS

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49
Q

Amino Acid chemical structure

A

.
H O
| ||
NH2—-C—-C–OH
|
R
Side chain

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50
Q

Amino acid not optically active

A

GLYSINE

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51
Q

amino acids along with their three-letter codes:

1.	Alanine 
2.	Arginine 
3.	Asparagine 
4.	Aspartic acid 
5.	Cysteine
A

amino acids along with their three-letter codes:

1.	Ala
2.	Arg
3.	Asn
4.	Asp
5.	Cys
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52
Q

amino acids along with their three-letter codes:
6. Glutamine
7. Glutamic acid
8. Glycine
9. Histidine
10. Isoleucine

A
  1. Gln or Q
  2. Glu or E
  3. Gly or G
  4. His
  5. Ile
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53
Q

amino acids along with their three-letter codes:
11. Leucine
12. Lysine
13. Methionine
14. Phenylalanine
15. Proline

A
  1. Leu
  2. Lys
  3. Met
  4. Phe
  5. Pro
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54
Q

amino acids along with their three-letter codes:
16. Serine
17. Threonine
18. Tryptophan
19. Tyrosine
20. Valine

A
  1. Ser
  2. Thr
  3. Trp or W
  4. Tyr
  5. Val
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55
Q

The one letter code for tryptophan

A

W

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56
Q

The one letter code for glutamic acid

A

E

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57
Q

Amino acids which are not synthesized by the body

A

Essential amino acids

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58
Q

10 essential amino acids

A

PVT TIM HALL
always ARGues never TYRes
1. Phenylalanine (Phe)
2. Valine (Val)
3. Threonine (Thr)
4. Tryptophan (Trp)
5. Isoleucine (Ile)
6. Methionine (Met)
7. Histidine (His)
8. Arginine (Arg)
9. Leucine (Leu)
10. Lysine (Lys)

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59
Q

Semi essential amino acids

A

HArg

HISTIDINE
ARGININE

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60
Q

Amino acids that undergoes glucogenic/ketogenic metabolism

A

WIFY
Tryptophan- W
Isoliucine- I
Phenylalanine- F
Tyrosine- Y

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61
Q

Amino acids metabolic products

A

Glucogenic Metabolism - glucose
Ketogenic Metabolism- Acetyl CoA

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62
Q

Amino acids that undergo ketogenic metabolism

A

Leu Ly

Leucine
Lysine

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63
Q

Amino acids: Non polar alipathic R groups

A

Glycine
Alanine
Valine
Leucine
Isoleucine
Methionine

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64
Q

.
COOH-
|
H3N+—-C—–H
|
H

A

Glycine

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65
Q

.
COOH-
|
H3N+—-C—–H
|
CH3

A

Alanine

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66
Q

.
COOH-
|
H3N+—-C—–H
|
CH
^
CH3 CH3

A

Valine

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67
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH
^
CH3 CH3

A

Leucine

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68
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH2
|
S
|
CH3

A

Methionine

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69
Q

.
COOH-
|
H3N+—-C—–H
|
H—-C—-CH3
|
CH2
|
CH3

A

Isoleucine

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70
Q

Amino acids: Non polar AROMATIC R groups

A

Phenylalanin
Tyrosine
Tryptophan

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71
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
^
|o|
v

A

Phenylalanine

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72
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
^
|o|
v
|
OH

A

Tyrosine

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73
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|_
|_>NH
<__>

Indole ring

A

Tryptophan

74
Q

Amino acids: Polar uncharged R groups

A

ASP PRO SER THRE GLUT CYST

Asparagine
Proline
Serine
Threonine
Glutamine
Cysteine

75
Q

.
COOH-
|
H3N+—-C—–H
|
CH2OH

76
Q

.
COOH-
|
H3N+—-C—–H
|
H—-C—OH
|
CH3

77
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
SH

78
Q

.
COOH-
|
C—–H
^
H2N CH2
| |
H2C—–CH2

79
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
C
^
H2N =O

A

Asparagus na naglutathione

Asparagine

80
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH2
|
C
^
H2N =O

A

Glutamine

Asparagus na naglutathione

81
Q

Amino acids: Positively charged R groups

A

Basic/alkaline in nature

HIS ARGuments are LYS

Histidine
Arginine
Lysine

82
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH2
|
CH2
|
CH2
|
+NH3

83
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH2
|
CH2
|
NH
|
C=NH2
|
+NH2

84
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
C—–NH+
| >CH
C—–N
H

85
Q

Amino acids: negatively charged R groups

A

Acidic nature
Glutasp

Aspartate
Glutamate

86
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
COO-

87
Q

.
COOH-
|
H3N+—-C—–H
|
CH2
|
CH2
|
COO-

88
Q

How to determine net charge of AA in an environment with Ph given

A
  1. Isoelectric point/pH (Electrically neutral)
  2. IP is less than PH(given)
    = net charge is positive

3.IP is more than PH(given)
= net charge is negative

More is less, Less is more

89
Q

AA which is electrically neutral

A

Zwitterion

90
Q

For neutral AA:
To compute isolectic point (pI)
given pka1 and pka2

A

Average of pka’s

91
Q

For ACIDIC AA:
To compute isolectic point(pI)
given pka1, pka2 and Pka3

A

Average of 2 lowest pka’s

92
Q

For BASIC AA:
To compute isolectic point(pI)
given pka1, pka2 and Pka3

A

Average of the 2 highest pka

93
Q

Tryptophan codes

94
Q

Glutamine codes

95
Q

Codes for Asparagin

96
Q

End product of glycogenolysis

A

GLUCOSE- liver
GLUCOSE-6-PHOSPHATE- muscle

97
Q

End product of pentose phosphate pathway/ HMP SHUNT

A

NADH
RIBOSE-5-phosphate

98
Q

AA structure not affected by denaturation process

A

Primary structure
Only destroyed by hydrolysis

Stabilized by peptide bonds

99
Q

Alpha helix 3.6 no of amino acids per turn
ex. Keratin

Beta pleeted sheet helix ex. Amiloid

Stabilized by Hydrogen bond

A

Secondary structure enzyme

100
Q

3D structure or DOMAIN: AA

Ex. Fibrous
Globular

A

Tertiary Structure

101
Q

AA structure with Spatial arrangement
Stabilized by COVALENT interactions

A

Quaternary

102
Q

Are proteins that act as catalysts, are not consumed in the reaction and has specificity

103
Q

Dehydrogenase is an example of enzyme(category) that TRANSFER electrons, which also result in change of oxidation state

A

OXIDOREDUCTASE

104
Q

Phosphorylase and kinase is an example of enzyme(category) that transfer FUNCTIONAL GROUP from one molecule to another

A

TRANSFERASE

105
Q

Protease, phosphatase is an example of enzyme(category) that BREAKDOWN covalent bond using water

106
Q

Decarboxylase is an example of enzyme(category) that BREAKDOWN covalent bond WITHOUT water or oxidation

107
Q

Mutase is an example of enzyme(category) that REARRANGEMENT of bond within a molecule

108
Q

An enzyme(category) that cause FORMATION of COVALENT BETWEEN 2 large molecule

109
Q

Plot used in enzyme kinetics

A

MICHAELIS-MENTEN PLOT

110
Q

MICHAELIS-MENTEN PLOT
Enzyme velocity increase as (V1)
Substrate concentration increases (S)

A

1st order kinetics

111
Q

MICHAELIS-MENTEN PLOT- (order kinetics)
Enzyme velocity increase as (V1)
Substrate concentration (S) remains CONSTANT at Vmax

A

Zero order kinetics

112
Q

MICHAELIS-MENTEN PLOT
Km or MICHAELIS-MENTEN constant= Affinity
Point where 1/2 of Vmax meet S

Relationship between Km & Affinity

A

⬆️Km= ⬇️ Affinity

⬇️Km= ⬆️ Affinity

113
Q

Plot used to determine
Vmax & Km
(Enzyme kinetics- Inhibition)

A

LINEWEAVER-BURK Plot

114
Q

LINEWEAVER-BURK Plot
Which type of inhibition is described as enzyme binding on ACTIVE site
Vmax= NA
Km= ⬆️

A

Competitive inhibition

115
Q

LINEWEAVER-BURK Plot
Which type of inhibition is described as enzyme binding on ALOSTERIC site
Vmax= ⬇️
Km= NA

A

Non competitive inhibition

116
Q

LINEWEAVER-BURK Plot
Which type of inhibition is described as enzyme binding on ENZYME SUBSTRATE site
Vmax= ⬇️
Km= ⬇️

A

Uncompetitive inhibition

117
Q

In enzyme structure apoenzyme(protein) + cofactor(non protein) will yeild

A

HOLOENZYME

118
Q

Cofactor composed of organic compounds is called

A

COENZYME
Loosely/temporarily attached to APOenzyme

119
Q

Coenzyme composed of inorganic compounds is called

A

PROSTHETIC GROUP
Permanently attached to APOenzyme

120
Q

Coenzyme Derived from Pantothenic Acid (Vitamin B5)

A

Coenzyme A (CoA)

121
Q

Coenzyme Derived from Niacin (Vitamin B3)

A

Nicotinamide Adenine Dinucleotide (NAD):

122
Q

Coenzyme Derived from Niacin (Vitamin B3)

A

Nicotinamide Adenine Dinucleotide Phosphate (NADP)

123
Q

Coenzyme Derived from Riboflavin (Vitamin B2)

A

Flavin Mononucleotide (FMN)

124
Q

Coenzyme Derived from Pyridoxine (Vitamin B6)

A

Pyridoxal Phosphate (PLP)

125
Q

Coenzyme Derived from Folate (Vitamin B9)

A

Tetrahydrofolate (THF)

126
Q

Coenzyme that Acts as a coenzyme in various reactions

A

Cobalamin (B12)

127
Q

Coenzyme that Acts as a coenzyme in carboxylation reactions

128
Q

Coenzyme that Plays a role in some enzymatic reactions, acting as a cofactor rather than a coenzyme.

A

Ascorbic Acid (Vitamin C)

129
Q

In gycolysis, the conversion of dihydroxyacetone phophate to glyceraldehyd 3-phophate is facilitated by which enzyme?

A

TRIOSE phosphate ISOMERASE
Yielding 2 molecules

130
Q

In Kreb’s cycle, the Starting point on which the pyruvate join the cycle is at the conversion of ______ to citrate by the enzyme citrate synthase

A

OXALOACETATE

131
Q

In Kreb’s cycle, What is the substrate which is converted from Citrate?

132
Q

These are polymers of NUCLEOTIDES joined by phosphodiester bonds

A

NUCLEIC ACIDS

133
Q

Nucleotide composition

A

Phosphate- Pentose sugar- Nitrogenous Base

134
Q

NucleoSIDE composition

A

Pentose sugar- Nitrogenous Base

135
Q

Nitrogenous base in Nucleotides could be either

A

PYRIMIDINE ^\N
|| |
V/
N
PURINE
N_ ^\N
// || |
\ N / \N//
H

136
Q

Pentose sugar in Nuceleotide could be either

A

RIBOSE
DEOXYRIBOSE

137
Q

Difference point between RIBOSE and DEOXYRIBOSE is on Carbon 2 functional group

A

Ribose- OH
Deoxyribose- H

138
Q

In nucleotides, what is the bond connecting Nitrogenous base to sugar

A

GLYCOSIDIC BOND

139
Q

In nucleotides, what is the bond connecting phosphate to sugar

A

ESTER BOND

140
Q

In nucleotides, what is the bond connecting a nucleotide subunit to another nucleotide subunit

A

PHOSPHODIESTER BOND

141
Q

In nucleotides, what is the bond connecting 2 nitrogen bases together (base pairing)

A

HYDROGEN bonds

142
Q

In DNA, How many Hydrogen bonds are there in A-T and C-G pairing

A

Adenine-thymine 2 H-bonds
Cytosine- Guanine 3 H-bonds

143
Q

What are the Pyrimidine Nitrogen Bases

A

CUT the Pyramid

CYTOSINE
URACIL
THYMINE

144
Q

What are the Purine Nitrogen Bases

A

PurGA

GUANINE
ADENINE

145
Q

Composition of pyrimidine nitrogen base CYTOSINE

A

Pyrimidine- NH2

cy2sine

146
Q

Composition of pyrimidine nitrogen base URACIL

A

Pyrimidine- O

Oracil

147
Q

Composition of pyrimidine nitrogen base THYMINE

A

Pyrimidine- O + CH3

OCHymine

148
Q

Composition of PURINE nitrogen base ADENINE

A

Purine - NH2

adeNHine

149
Q

Composition of PURINE nitrogen base GUANINE

A

Purine- O + NH2

gOaNHine

150
Q

What PYRIMIDINE bases are exclusively found in DNA & RNA respectively

A

DNA- Thymine
RNA- Uracil

Both PURINES A&G are found in D/RNA

151
Q

What type of DNA 🧬 is left Handed

A

Z DNA

A/B are right handed

152
Q

Number of turns/twists in DNA types A,B,Z

A

A has 11 (Aleven) ALANG tubig DEHYDRATED
B has 10 BASA HYDRATED

Z has 12 (Zuelve)

153
Q

RNA that Carries genetic information from the DNA in the cell nucleus to the ribosomes in the cytoplasm. It serves as a template for protein synthesis during translation.

A

Messenger RNA (mRNA)

154
Q

RNA that Transfers amino acids to the ribosome during protein synthesis

A

Transfer RNA (tRNA):

155
Q

RNA that Forms a major part of the ribosomes, where protein synthesis occurs. It helps in the binding of mRNA and tRNA during translation.

A

Ribosomal RNA (rRNA

156
Q

RNA structure consisiting of:

5’ CAP
POLY (A)tail

Also contains CODON

A

🧢
mRNA🪡

157
Q

Clover shape RNA structure, consisiting of:

5’
D arm loop
Anticodon arm
3’CCA Acceptor arm

158
Q

Support or hold together tRNA & mRNA

SUPPORTING ACTORS

159
Q

Process by which DNA is transformed to RNA

A

Transcription

160
Q

Process by which RNA is transformed to PROTEIN

A

TRANSLATION

161
Q

Enzymes in DNA replication

A

Helicase- unwind the strand from inside the bubble

Topoisomerase- relieves tension on parent chain to allow unwinding

DNA polymerase- assembles new DNA

DNA Ligase- connects okazaki fragments from lagging strand

162
Q

DNA Transcription steps

A

INITIATION
ELONGATION
TERMINATION

163
Q

Enzymes in RNA transcription (mRNA)

A

RNA polymerase- binds to TATA box (promoter region of DNA) then unwind the strand - INITIATION of mRNA

mRNA- transcription/ ELONGATION

AAAAAA- TERMINATION point

164
Q

PROCESSING occur after mRNA transcription before releasing into CYTOSOL for translation.

The following are the modifications:

A
  1. 5’ CAP addition- stability, binding site of ribosomal subunit for protein synthesis
  2. POLY-A tail addition- for motility
  3. INTRONS deletion- non coding region
  4. EXONS connection- coding region
165
Q

TRANSLATION or protein synthesis
tRNA will start in the Attachment of AA to 3’ = aminoacyl-tRNA (powered by GTP). The translation processes are:

A
  1. INITIATION- 3 bases (codons)
    -mRNA Start CODON- AUG (MET)
    -tRNA ANTICODON- UAC
    -Small ribosomal unit
  2. ELONGATION- big ribosomal unit will attach, tRNA will bind to/release from the ribosome complex (repeatedly) until elongation is complete
  3. TERMINATION- STOP codon
    UGA
    UAG
    UAA
166
Q

Final modification of Protein synthesis occurs in

A

Golgi appratus

167
Q

The rules stating:

DNA contains
Adinine = Thymine
Cytosine=Guanine
Purine=pyrimidine

A

CHARGAFF’s rule

168
Q

Generic code characteristics

A
  1. Degenerate
  2. Unambigous
  3. Non overlapping
  4. Universal
169
Q

DNA base pairing rule:

A
  1. Adenine (A) always pairs with Thymine (T), forming two hydrogen bonds.
  2. Guanine (G) always pairs with Cytosine (C), forming three hydrogen bonds.
170
Q

Esters of fatty acids and alcohol

A

Fats/ Oils

171
Q

Bond that stabilize triacylglycerol (triglycerides)

A

Ester bond

172
Q

Reaction that combine fatty acids and glycerol

A

DEHYDRATION

173
Q

Triacylglycerol (triglycerides) are derived ( liver/ adipose glycolysis) from DHAP(Dihydroxyacetone phosphate) to?

A

Glycerol phosphate

174
Q

TAG (triacylglycerol) is produced from glycerol phosphate by

A

Linking of FA to glycerol by ACETYLTRANSFERASE

X3

175
Q

Hydrolysis of stored fat is

A

LIPOLYSIS

By TAG-lipase releasing FREE FA
- Beta oxidation - producing 106/131 ATP

176
Q

Rate limiting step in LIPOLYSIS

A

Carnitine palmitoyl transferase

177
Q

What is the complex lipid consisting of:

Glycerol backbone
3 fatty acids

(Breakdown products)

A

TRIACYLGLYCEROL

178
Q

Complex lipid consisting of:

Glycerol backbone
2 fatty acids
1 phosphate head group

(Breakdown products)

A

GLYCEROPHOSPHOLIPIDS
Ex. Phosphatidylcholine, serine, ethanolamine, etc

179
Q

Complex lipid consisting of:

GlyceroEther backbone
1 fatty acids
1 phosphate head group

(Breakdown products)

A

Ether glycerolipids
Ex. Plasmalogens

180
Q

Complex lipid consisting of:

Sphingosine backbone
1 fatty acids
1 phosphate head group

(Breakdown products)

A

SPHINGOPHOSPHOLIPIDS
Ex. Sphingomyelin

181
Q

Complex lipid consisting of:

Sphingosine backbone
1 fatty acids
1 CARBOHYDRATE

(Breakdown products)

A

GLYCOLIPIDS
Ex. Cerebrosides, Sulfatides, Globosides, Gangliosides

KAPS Paper 1 (4 decks)

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