Biology 1 - Disease to Proteins Flashcards

(51 cards)

1
Q

Antigen

A

A protein that stimulates an immune response resulting in the production of antibodies

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

Polymer

A

large molecules made by joining many identical monomers

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

Primary structure of protein

A

The order in which amino acids are arranged

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

Mitochondria

A

Deeply folded inner membrane

Perform aerobic respiration and produce ATP

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

Cell fractionation and Ultracentrifugation

A
  1. Homogenise cell to break it open
  2. Filter solution
  3. Centrifuge at low speed to separate largest organelle
  4. Remove pellet and centrifuge at higher speed.
  5. Repeat a higher speeds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Why use a buffered solution in cell fractionation?

A

To prevent pH changes that could damage organelles by denaturation

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

Why use an ice cold solution in cell fractionation?

A

To reduce enzyme activity

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

Golgi Apparatus

A
  • Layers of flattened fluid filled sacs
  • Proteins/ lipids produced by ER pas through
  • Sorts, modifies and packages molecules into vesicles
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Ribosomes

A

Found all over cell but mainly on Rough Endoplasmic Reticulum
Perform protein synthesis
Prokaryote: 70s
Eukaryote: 80s

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

Rough Endoplasmic Reticulum

A

Encrusted with ribosomes

Site of protein synthesis

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

Smooth Endoplasmic Reticulum

A

Synthesises lipids

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

Secondary Protein Structure

A

Polypeptide chain folded into alpha helixes or beta pleated sheets

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

Tertiary Structure of Proteins

A

3D shaped molecule made by hydrogen, ionic and disulphide bonds between R groups.
Disulphide bonds between cysteines only

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

Lysosomes

A

Vesicles that contain digestive enzymes

Hydrolyse worn out organelles and pathogens

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

Scanning Electron Microscope

A
Sample does not need to be thin
3D image
Lower resolution
Dead sample
Black and white image
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Quaternary Protein Structure

A

2 or more polypeptides joined together

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

Transmission Electron Microscope

A
High resolution
High magnification
2D image
Dead sample
Thin sample
Black and white image
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

How do pathogens cause disease?

A

Release toxins

Direct damage to cells

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

Antibodies

A

Protein made in response to a foreign antigen.

Have binding sites specific to antigen

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

Production of Monoclonal Antibodies

A
  1. Inject mouse with disease to start immune response.
  2. Isolate B cells and fuse with tumour cells
  3. Antibodies isolated then cloned
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Vaccination

A

A dead, weakened or attenuated sample if a pathogen that initiate an immune response and the production of memory cells.

22
Q

Biuret Test

A

For proteins
1. Add sodium hydroxide solution
2.Add copper sulphate solution
colour change from clear blue to violet if protein present

23
Q

Emulsion Test

A

For lipids
1. Add ethanol
2. Add water
turns cloudy if lipids present

24
Q

Monosaccharides that make up carbohydrates are…

A

Glucose
Fructose
Galactose

25
How are carbohydrates joined and what bond is formed?
Condensation reaction and glycosidic bond is formed.
26
Benedict's Test
``` For reducing sugars 1. Boil sample with benedict's reagent 2. Coloured precipitate formed if reducing sugar present. Red ppte - much sugar Green ppte- small amount of sugar ```
27
Test for Non Reducing sugars
1. Heat with dilute acid 2. Add sodium hydrogen carbonate to neutralise. 3. Test with benedicts as you would with reducing sugar, should give positive result
28
Which parts of the body are most vulnerable to infection and why?
Gas exchange system and lining of the digestive system They are in contact with the environment at all times Have a large surface area Have a thin exchange surface.
29
Risk factor
factors that increase the chance of developing a disease.
30
Factors that increase the risk of cancer
Exposure to ionising radiation | Exposure of carcinogenic chemicals
31
Factors that increase the risk of CHD
``` Lack of exercise High lipid diet Smoking High cholesterol diet Stress High blood pressure ```
32
Percentage change
Change ------------ x 100 Original
33
Describe question points
Say what you see Give an overall trend State any significant changes in data Use data from graph/table in answer
34
Data handling question answers
Must be balanced | Give a reason why correlation may not show causation
35
Stages of Protein Synthesis
``` Nucleus Ribosomes Rough Endoplasmic Reticulum Golgi Vesicles ```
36
How to calculate magnification
``` Image size ---------------- Object size Always measure in mm Convert answer into micrometers ( x1000) ```
37
Stages of phagocytosis
1. Phagocyte follows chemoattracants released by pathogen. 2. Phagocyte engulfs pathogen. 3. Pathogen enclosed in vesicle. 4. Lysosome fuses with vesicle and releases digestive enzymes that hydrolyse pathogen. 5. Waste material ejected from cell.
38
Cellular response to infection
1. Antigen presents pathogen antigens on cell surface after phagocytosis. 2. T cell binds to antigen. 3. t cell activated and clones to help fight infection.
39
Humoral response to infection
1. T cell binds to presented antigen and activates B cell. 2. T cell releases chemicals that signal to the B cell to clone into plasma cells and Memory cells by mitosis. 3. Plasma cells produce antibodies 4. Memory cells remain in the body to fight future re- infections.
40
Secondary Response
Memory cells producing antibodies to fight a re-infecton of a disease. More antibodies are produced more quickly.
41
Antigenic Variability
Some pathogens have antigens that mutate and change shape e.g. influenza making it more difficult to produce a vaccine for that disease because the pathogen will not be recognised by memory cells.
42
What is passive immunity
Antibodies are received from elsewhere i.e. are not produced by an individual. Can be given by mother or an injection.
43
What is active immunity
Immunity provided by memory cells produced by a primary response to a pathogen.
44
What is a disadvantage of using an attenuated vaccine?
Vaccine may mutate into full version of virus and patient may need to fight a full infection
45
Herd Immunity
Lots of individuals are vaccinated so there is little chance of the disease spreading because there is a low chance that non vaccinated people will come into contact with the disease.
46
Immune response mark points
1. Vaccine contains sample of pathogen. 2. Phagocyte hydrolyses pathogen and presents antigens. 3. T cell binds to antigen. 4. T cell activates B cell 5. B cell divides into plasma and memory cells. 6. Vaccine stimulates primary response. 7. Memory cells produced give rapid response to future re infections.
47
Why antibodies target and bind to only one antigen?
Complementary and specifically shaped binding site. | Antigen - antibody complex formed.
48
What chemical elements do all protein and amino acids contain?
Carbon, Hydrogen, Oxygen, Nitrogen
49
What are names and formulae of the two groups in the general structure of an amino acid?
Amino group - NH2 | Carboxylic Acid group - COOH
50
What molecules are formed in a condensation reaction between two amino acids?
Dipeptide molecule and water
51
Explain how a change in the primary structure of a protein may result in a different 3 dimensional structure.
1. change in primary structure leads to a change in the sequence of amino acids. 2. Therefore change in secondary structure and change in the position of bonds between R groups in tertiary structure. 3, Change in position of hydrogen, ionic and disulphide bonds so change in 3D structure.