Biochemistry Flashcards

1
Q

What are nucleotides?

A

Compound = nitrogen containing base + sugar + phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Which end of DNA are new nucleotides added to?

A

3”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are ZDV & AZT?

A

Retrovirals (used to treat HIV)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are Okazaki fragments?

A

Short DNA formed on a lagging strand in DNA replication

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What does helicase do?

A

Unwind DNA strand (stop it rewinding)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

In which direction is the leading strand formed in?

A

3” - 5”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

In which direction is the lagging strand formed in?

A

5” - 3”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What do enzymes do?

A

Catalyse a reaction so it reaches equilibrium faster

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Do enzymes alter the position of equilibrium?

A

No

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are the 2 types of co factors?

A

Metal ions

Coenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is an apoenzyme?

A

Enzyme without cofactor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is holoenzyme?

A

Enzyme with cofactor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Where do substrates bind to enzymes?

A

Active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What factors affect enzyme activity?

A

Temperature
pH
Concentration (enzyme or substrate)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are isozymes?

A

Isoforms of enzymes

Catalyse same reaction but have different shape & properties

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What does increased CK show?

A

Muscle damage (skeletal)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are Zymogens?

A

Inactive precursors of enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What does the Michaelis-Menten equation show?

A

Kinetics of an enzyme reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is Vmax?

A

Maximal rate of reaction (with unlimited substrate)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is Km?

A

Michaelis constant

Conc of S when 1/2 Vmax

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Mechanisms of enzyme control

A
Allosteric 
Regulation of transcription 
Reversible covalent modification 
Irreversible covalent modification 
Degradation
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is Allosteric control?

A

Altered enzyme activity by means of conformation induced by different molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Do Allosteric enzymes follow Michaelis-Menten kinetics?

A

NO

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What shape is the curve of an allosteric enzyme?

A

Sigmoid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What is cooperativity?
Influence that binding of a ligand to one promoter has on the binding of a ligand to another promoter in an oligomennorhea phase
26
What are nucleosides?
Compound = nitrogen based base + sugar | E.g. Adenosine
27
4 types of amino acid
Polar Non polar Acidic Basic
28
What is the Henderson-Hasselbach equation used for?
Calculate the properties of buffer solutions
29
What is a buffer solution?
A solution that's pH remains constant when small amounts of acid or base are added
30
When does pH = pKa in a titration curve?
Point of inflexion
31
What is the primary structure of a protein?
Sequence of amino acid residues (held together by covalent peptide bonds)
32
What is the secondary structure of a protein?
Localised conformation of the polypeptide backbone
33
What is the tertiary structure of a protein?
3D structure of an entire polypeptide, including all its side chains
34
What is the quaternary structure of a protein?
Spatial arrangement of polypeptide chains in a protein with multiple subunits (NOT all the time)
35
3 arrangements of secondary structure protein?
Alpha helix Beta pleated sheets Beta strands
36
Which protein has a triple helix?
Collagen
37
Why is collagen important?
Influences strength of connective tissue | Important for blood clotting
38
Symptoms of scurvy?.
Bleeding gums | Skin discolouration
39
Stages of catabolism
1) macromolecules -> monomeric units 2) monomeric units -> Acetyl-CoA + some ATP 3) Acetyl group -> Kreb cycle -> CO2 + H2O
40
3 types of protein
Fibrous Globular Conjugated
41
Which forces stabilise tertiary structures?
``` Covalent disulphide bridges Electrostatic interactions Hydrogen bonds Hydrophobic interactions Complex formation with metal ions ```
42
What 4 things can disrupt protein structure?
Heat Extremes of pH Detergents (urea, guanidine hydrochloride) Thiol agents, reducing agents
43
Where does GLUT1 work?
Brain (low Km)
44
Where do GLUT2 receptors act?
``` Liver (high Km) Beta cells (insulin dependent) ```
45
Where does the GLUT3 receptor act?
Brain (low Km)
46
Where does the GLUT4 receptor act?
Muscle (insulin-dependent) | Adipose tissue
47
Where does the GLUT5 receptor act?
But (fructose transport)
48
3 enzymes involved in glycolysis?
Hero kinase Phospofructokinase Pyruvate kinase
49
What is the substrate for the TCA cycle?
Acetyl Co-A
50
What is given off when pyruvate is converted to Acetly Co-A?
CO2
51
What combines with Acetyl Co-A at the start of the TCA cycle?
Oxaloacetate
52
How many GTP are produced in the TCA cycle?
1
53
What are the 2 stages of oxidative phosphorylation?
Electron transport | ATP synthesis
54
In oxidative phosphorylation what reduces O2 to H2O?
Electrons from NADH & FADH
55
What does the P/O ratio measure?
The coupling of ATP to synthesis to electron transport
56
How many ATP are made in total in the complete oxidation of glucose?
30-32 ATP molecules
57
What type of diseases are OXOPHOS?
Degenerative diseases
58
Examples of glycogen storage disease
McArdle's disease Andersen disease Pompe disease
59
Which enzyme marks muscle damage and what is its presentation?
CK General aches/pains, crush injury, dark urine, poor exercise tolerance
60
What enzymes indicate liver damage and what is its clinical presentation?
ALT, AST, GGT Abdominal pain/tenderness, nausea/vomiting, jaundice
61
What enzymes indicate pancreatic damage and what does it present as?
AMY, LIP Acute abdominal pain, radiates to back
62
What enzymes indicate cardiac damage and what is its clinical presentation?
CK, AST, LDH Central chest pain, acute breathlessness, palpitations, cardiac arrest
63
What does an increase in ALT usually indicate?
Drug overdose (or liver necrosis) - exclusive to liver
64
What does GGT increase indicate?
GGT found in biliary tract and in liver | Increase shows alcohol excess
65
What is lipase a good indicator of?
Pancreatic hepatitis
66
What does reduced trope in show?
Had an MI
67
Symptoms of hyperglycaemia?
``` Extreme thirst Dry mouth Blurred vision Drowsiness Frequent need to pass urine ```
68
Symptoms of hypoglycaemia?
``` Feeling shaky and irritable Sweating Tingling lips Feeling weak Hunger Nausea ```
69
Why do hypoglycaemic patients feel sick?
Lack of glucose -> breakdown fats to ketones -> acidosis
70
What are chylomicrons?
A lipoprotein present in the blood after digested fat has been absorbed from the small intestine
71
How do statins work?
Inhibit an enzyme involved in cholesterol synthesis in the liver
72
How is Vmax determined from a Lineweaver-burk plot?
Intersection with the y axis
73
How is Km determined from a lineweaver-burk plot?
Intersection with x axis