Block 2 Lecture 7 & 8: Protein folding + Chemical Energy Flashcards

1
Q

To change from primary to secondary structure, which bonds must be formed between amino acid side chains?

A

Hydrogen bonds

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

what are the two kinds of secondary strucutre

A

alpha helix and beta pleated sheet

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

Tertiary structure involves the collapse of ______ components and the facing outwards of ______ components

A

the collapse of hydrophobic components and the facing outwards of hydrophilic components

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

what are the bonds present in tertiary structure between non-polar amino acid side chains, and how strong are they relatively

A

Van der Waals, weak

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

what bonds are present between polar side chains in a tertiary structure

A

hydrogen bonds

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

what bonds are there between charged amino acid side chains on a tertiary structure, and how strong are they relatively?

A

ionic bonds, weak

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

What structure of protein do disulphide bridges form and between what two molecules do they form?

A

form in a tertiary structure between two cysteine molecules. Is a strong bond

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

what does a quaternary structure consist of?

A

two or more polypeptide chains each with their own tertiary structure

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

homodimer and heterodimer complexes are part of which classification of protein structure?

A

quaternary

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

where are membrane anchored and secretory proteins initially translated?

A

on cytoplasmic ribosomes

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

What is the name of the particle that recognises the signal peptide when it emerges from the ribosome after being translated?

A

the SRP, signal recognition particle

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

what is the function of the SRP, the signal recognition particle?

A

targets specific receptors in the ER membrane

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

is the signal sequence found at the C terminus or the N terminus of the polypeptide chain?

A

the N terminus

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

what is the process for the translocation of a secretory protein (e.g a hormone) across the ER membrane?

A

chain is completely translocated and the signal sequence is cleaved off by a signal peptidase.

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

Do secretory proteins remain insoluble in the ER lumen once they have been translocated?

A

No, they are effectively solubilised in the lumen once they have been translocated.

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

What is the process for the transaction of a membrane protein across the ER membrane?

A

one or more of the hydrophobic segments of the polypeptide chain anchors it in the bilayer

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

Which of membrane and secretory proteins are moved via transport vesicles from the ER to the Golgi?

A

Both membrane and transport proteins are moves via transport vesicles from the lumen of the ER to the Golgi

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

What are the different types of vesicles that operate from the Golgi?

A

Transport vesicles which move proteins to lysosomes, Membrane vesicles which merge proteins to the membrane of the cell, secretory vesicles which export proteins out of the cell via exocytosis.

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

Which face of the Golgi are vesicles packaged at?

A

The trans face of the Golgi

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

______ reactions transfer energy from complex molecules to ATP

A

catabolic

21
Q

______ reactions transfer energy from ATP to complex molecules

A

anabolic

22
Q

do catabolic or anabolic reactions result in the storage of energy

A

catabolic

23
Q

what facilitate the transfer of glucose from the bloodstream into a cell?

A

insulin

24
Q

what facilities the conversion of stored glucose, as glycogen, to glucose in the bloodstream?

A

glucagon

25
Q

Is glycolysis anaerobic or aerobic and where does it occur?

A

anaerobic, occurs in the cytoplasm

26
Q

what is the reactant and what is the product of glyoclysis

A

Glucose turns into two molecules of pyruvic acid and four ATP

27
Q

How many ATP are used in the process of glycolysis

A

2 ATP

28
Q

How many NAD molecules are reduced by glycolysis

A

2

29
Q

what must happen in between glycolysis and the Krebs cycle?

A

the formation of Acetyl CoA

30
Q

How is Pyruvic acid converted to Acetyl CoA

A

aerobic process in the mitochondrial matrix

31
Q

is the formation of Acetyl CoA anaerobic or aerobic

A

aerobic, requires O2

32
Q

What does the Krebs Cycle produce from 1 molecule of Acetyl CoA

A

1 x ATP,
2 x CO2,
1 x FADH2 and 3 x NADH

33
Q

Where does the Krebs Cycle occur and is it an aerobic or anaerobic process?

A

in the mitochondrial matrix, is aerobic

34
Q

During the electron transport chain, what does the enzyme ATP synthase do as protons move back across the mitochondrial membrane?

A

Phosphorylate ADP to ATP

35
Q

what is the final electron acceptor in the electron transfer chain

A

O2, forms water

36
Q

ETC uses energy from _____ reactions to fuel pumping of protons up a concentration gradient from matrix to inner membrane space

A

redox

37
Q

what is proton motive force derived from

A

the energy rich electrochemical gradient

38
Q

how many protein complexes form the ETC?

A

4

39
Q

what two kinds of phosphorylation are present during cellular respiration?

A

substrate level phosphorylation (Krebs and Glycolysis) and oxidative phosphorylation (ETC)

40
Q

Does NAD+ or FAD promote the production of more ATP

A

NAD

41
Q

where is insulin produced

A

by beta cells of Islets of Langerhans in pancreas

42
Q

what is the function of insulin

A

promote glucose uptake into cells (for ATP production or storage in liver). insulin produced when blood sugar levels are high

43
Q

where is glucagon produced

A

Produced by alpha cells of Islets of Langerhans in pancreas

44
Q

what is the function of glucagon

A

Stimulates the breakdown of glycogen to increase blood sugar levels

45
Q

Diabetes Mellitus : a disease in which the body’s ability to produce or respond to the hormone____ is impaired, resulting in abnormal metabolism of carbohydrates and _____ levels of glucose in the blood.

A

insulin, results in elevated/increased levels of glucose in blood

46
Q

what is the difference between type 1 and type 2 diabetes

A

type 1: beta cells of pancreas are destroyed so insulin is not produced.

type 2: body produces insulin but receptors are non-functional

47
Q

what is the most common form of diabetes

A

type 2

48
Q

what are some side effects of diabetes

A

excessive thirst, frequent urination, weight loss, fatigue