Topic 1 Flashcards

1
Q

General formula of carbohydrates

A

Cx(H2O)n

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

Characteristics of glucose

A

C6H12O6
Monosaccharide
Heroes sugar- it has only 6 carbons + has a ring structure

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

Draw a- glucose molecule

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

Draw a B- glucose molecule

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

Draw molecule of ribose

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

Formula of maltose

A

Maltose is not 2x glucose because water is lost in the formation of glycosidic bonds

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

How disaccharides are formed

A

Condensation reaction when water is lost
They form 1,4 glycosidic bonds - draw it

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

How disaccharides are split

A

Through hydrolysis reaction when water is added to break glycosidic bonds

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

Examples of disaccharides

A

Maltose- 2 a- glucoses
Sucrose- glucose and fructose
Lactose- B- glucose and galactose joined with B 1,4 glycosidic bonds

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

Examples of polysaccharides

A

Starch- mixture of amylopectin and amylose
Glycogen- carbohydrate energy store found in animals

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

Properties of starch

A

A- glucose polymer

Starch contains amylose which is a straight chain coiled by hydrogen bonds which makes a compact store of glucose and therefore energy

In amylopectin there are branches of 1,6 glycosidic bonds which allows a little bit of coiling, so amylopectin is more easily broken down than amylose

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

Properties of glycogen

A

Similar to amylopectin but with more frequent branches of 1,6 glycosidic bonds which allowed faster release of energy

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

Properties of cellulose

A

B- glucose polymer

Chains don’t coil, but they lie next to each other

Alternating unit inversion allows hydrogen bonding between OH groups in one area and O atoms in other areas of the molecule. These hydrogen bonds hold chains together to form strong microfibrils

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

Properties of lipids

A

Hydrophobic
Made up of fatty acids and glycerol

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

Name of bonds formed between fatty acids and glycerol

A

Ester bonds

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

Draw a diagram of triglyceride

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

Difference between saturated and unsaturated fatty acids

A

Saturated fatty acids are straight chains
Unsaturated fatty acids have a kink at each double bond which makes them less compact and will be liquid at room temperature

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

Draw a phospholipid

A

Hydrophilic head
And 2 hydrophobic tales

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

Energy from lipids

A

Ideal long term store of energy
Lipids release more energy than carbohydrates
More C-O bonds are made when lipid is respired
Lipids are also insoluble so can travel in body

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

Lipids functions in the membrane

A

Delimit the cell
Form the main barrier to movement in and out the cell
Allow embedding of membrane proteins which allows movement of molecules
Membrane fluidity allows cell to change shapes, fluid membranes contain more unsaturated fats

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

Which bonds join amino acids

A

Peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Draw a lab led diagram of amino acid

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

Draw amino acids after condensation reaction

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

What is the primary structure of a protein

A

Sequence of amino acids forming a polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What is secondary structure of a protein
When polypeptide chains are held together by many hydrogen bonds forming an a- helix or B- pelted sheet
26
What is tertiary structure of a protein
A- helix or B- pelted sheet fold further to give it unique tertiary structure. Folds are held by hydrogen, ionic and disulphide bonds between R groups
27
What is a quaternary structure of a protein
When different folded chains join together by the same type of bonds as in tertiary structure
28
How hydrogen bonds are formed in proteins
Amino (positive) and carboxylic acid (negative) groups carry small amounts of charge. This forms hydrogen bonds
29
Properties of collagen
Fibrous protein There are 3 a- helices which are held by a large number of hydrogen bonds and bind very tightly because every third amino acid is a small glycine which can fit into the very small space on the inside of triple helix On the either side of the glycines are proline and hydroxyproline which have big R groups, these groups keep out of each others way to maintain the strong, insoluble fibrous structure Collagen molecules cross- link with one another, providing further strength
30
Properties of Haemoglobin
Globular protein Found in red blood cells and responsible for binding and releasing of oxygen 4 polypeptide chains- 2 a and 2 b and have 1 haem prosthetic group in each which contain iron to bind with oxygen
31
Substitution mutation
When one nucleotide is changed to another Consequences are usually minor as only one amino acid is changed and all codons remain in frame
32
Consequences of deletion and insertion
Usually major as every amino acid after the mutation is changed due to frame shift effect
33
What is deletion mutation
When one amino acid disappears from the code
34
What is insertion mutation
When 1 base pair is inserted in a genetic code
35
Draw a nucleotide diagram
36
How many bonds between base pairs
2 hydrogen bonds between A and T 3 hydrogen bonds between C and G
37
How many base pairs are there in each complete twist
10
38
What does it ben that DNA is anti parallel
One strand is going to 3 to 5 direction and the other one is 5 to 3 direction
39
Which Penrose DNA has
Deoxyribose
40
What are the purines
A and G
41
What are pyrimidines in DNA
C and T
42
Bonds in DNA
Phosphodiester bonds
43
Penrose in RNA
Ribose
44
Purines and pyrimidines in RNA
Purines: A and G Pyrimidines: C and U
45
How RNA structure is related to its function
RNA is small so can pass out of the nucleus into the cytoplasm
46
Differences between mRNA and tRNA
mRNA is usually not folded and tRNA is folded into a specific pattern held by hydrogen bonds mRNA carries codons and tRNA anticodons
47
How anaemia occurs
Base substitution results in a single amino acid change in the B- glob in polypeptide chains (valine replaces glutamic acid)
48
How anaemia affects haemoglobin
Haemoglobin carriers oxygen in the blood. In sickle cell anaemia there is a mutation in one base of the codon, this changes shape of a red blood cell so its less efficient in carrying oxygen. This can cause tiredness, blocked vessels and even death
49
Why red blood cells are sickle- shaped
Glutamic acid in the B- globin polypeptide chain is replaced with valine. Valine is less soluble which causes changes in Haemoglobin and it becomes long rigid chains which don’t transport oxygen as effectively
50
Practical: investigating rates of reaction
Protease is used to break down a cloudy protein solution—> it will become less cloudy—> decrease in cloudiness is measured with a colorimeter, taking an absorbance reading every few seconds—> results can be plotted as absorbance (y) agains time (x)—> gradient of a line can be calculated —> rate can be then calculated
51
What is a dependent variable
Thing to be measured
52
What is independent variable
What is manipulated eg amount of water or light
53
What is control variable
Variables which are kept constant eg species
54
What is competitive inhibition
Competitive inhibitor blocks active site. With excess substrate, substrate always occupies the site before the inhibitor can
55
What is non- competitive inhibition
Changes shape of the active site which decreases products
56
What is end product inhibition
When enzyme exists in an active form and inactive form, they are called allosteric enzymes. They are inhibited by the end product of a series of reactions. Enzyme becomes active again when more product is needed
57
Properties of water
High specific heat capacity because hydrogen bonds keep the temperature in bodies of water fairly constant High surface tension because of hydrogen bonds which helps some organisms to travel on water Incompressible which helps to create hydrosceleton in starfish It has maximum density at 4C which allows sie to float on the surface
58
Water facts based of dipole nature of water
H- positive and O- negative which makes water unevenly charged Water is liquid at room temperature Water easily dissolves charged molecules
59
Cell organisation
Specialised cell—> tissue—> organ—> organ system—> organism
60
Draw a bacteria
including 70s ribosomes, cell membrane, cell wall, nucleod, cytoplasm, plasmid, pili, capsule, flagellum
61
Function of plasmids
Contain genes which aid bacterium’s survival such as antibiotic resistance or genes for production of toxins
62
Ribosomes in prokaryotes
70S so made of 30S and 50S subunits, they make proteins
63
Cell wall in prokaryotes
Made of peptidoglycan In some bacteria peptidoglycan cell wall is very thick and protective and get stained purple - gram positive In others cell wall is thin and gets stained red. They also have additional fatty/proteins membrane- gram negative
64
Advantages of gram negative and positive bacteria
Gram negative bacteria are more resistant to antibiotics which act of wall formation Gram positive bacteria have thicker cell wall, which is protective