biological molecules Flashcards

1
Q

what is a monomer?

A

repeating subunits that make up a polymer

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2
Q

What is a polymer?

A

a chain of monomers

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3
Q

What is a condensation reaction?

A

Forming bonds between between monomers, water is produced

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4
Q

What is a hydrolysis reaction?

A

Breaking bonds between polymers, water used

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5
Q

Give two examples of biological polymers

A

Proteins
Polysaccharides

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6
Q

Give three examples of biological monomers

A

Monosaccarides
Amino acids
Nucleotides

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7
Q

What is the general formula for carbohydrates?

A

(CH2O)n

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8
Q

What are monosaccarides?

A

. Sweet tasting soluble substances
. Glucose, fructose, galactose

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9
Q

where is starch found and what is it made of?

A

. plants
. amylose and amyloplecin

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10
Q

what is the structure of starch?

A

. compact (due to coiled and branched chains)
. insoluble so does not effect osmotic properties of cell

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11
Q

what is the function of starch?

A

. storage of energy in plants
. lots of glucose can be fit in a small space due to coils

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12
Q

where is glycogen found and what is it made of?

A

. animals
. alpha glucose

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13
Q

what is the structure of glycogen?

A

. even more coiled and branched than amylopecin
. insoluble so does not effect osmotic properties of cell

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14
Q

what is the function of glycogen?

A

. main energy store in animals
. lots of glucose so can fit in small space due to coils

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15
Q

where is cellulose found and what is it made of?

A

. cell walls of plants
. beta glucose and hydrogen bonds

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16
Q

what is the structure of cellulose?

A

. long and unbranched
. held together by hydrogen bonds
. large numbers of beta glucose chains
. layers on top of eachother

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17
Q

what is the function of cellulose?

A

. structure
. many chains together in layers to form microfibril and fibril to keep cell wall strong

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18
Q

what is the structure of lipids?

A

. contains C,H,O
. O:C:H smaller than carbohydrates
. insoluble in water
. soluble in organic solvents (acetone and alcohol)
. tryglycerides and phospholipids

19
Q

how are lipids used in cell membranes?

A

. cell surface membrane and around organelles
. phospholipids contribute to flexibility of membranes and transfer of lipid-soluble substances

20
Q

how are lipids a source of energy?

A

. when oxidised, provide more than 2x energy of carbs and release valuable water

21
Q

how are lipids waterproof?

A

. insoluble in water, waxy lipid cuticles that conserve water
. mammals have oily sector

22
Q

how do lipids provide protection?

A

. stored in delicate organs such as kidney

23
Q

how do lipids provide insulation?

A

. slow conductors of heat, can help retain body heat
. act as electrical insulators around mylen sheath in nerve cells

24
Q

what are properties of tryglycerides?

A

. glycerol and 3x fatty acids
. condensation reaction for fatty acid bond
. ester bond with glycerol
. glycerol is the same in fats and oils
. variations in fatty acids
. over 70 different fatty acids
. all have -COOH group with hydrocarbon
. saturated= c-c
. unsaturated= c=c

25
what is the structure of phospholipids?
. 2 fatty acids and glycerol . inorganic phosphate group in place of 3rd fatty acid
26
how can phospholipids be described as polar?
in an aqueous environment, phospholipid molecules from a bilayer within cell surface membranes
27
how do they have hydrophyllic heads?
faces water and helps to hold at cell surface membrane
28
What can be made of proteins?
. Hair and skin contain a protein called keratin . They make haemoglobin (o2 carrying RBC) . Bones contain a protein called collagen . Hormones such as insulin are often proteins . Found in cell membranes
29
How many different amino acids are there?
20
30
What are primary structure proteins?
The sequence of amino acids in a polypeptide or protein
31
What are secondary structure proteins?
The regular folding or coiling of the polypeptide chain due to the formation of hydrogen bonds
32
What are tertiary structure proteins?
The unique 3D folding of the polypeptide chain
33
What are quaternary structure proteins?
The 3D arrangement of 2 or more polypeptide chains, often involving a prosthetic group
34
What are the qualities of enzymes?
Increased temperature makes molecules move faster Biological systems are very sensitive to temperature changes Increase RoR without increasing temp Create a new reaction pathway "short cut"
35
What is free energy?
Energy available the enzymes need to perform work
36
What is the structure of enzymes?
Have a specific 3d shape Specific region of enzyme is functional- active site Small depression in enzyme molecule Substrate fits into depression to form enzyme-substrate complex Substrate is held by temporary bonds that form between certain amino acids of active sites and groups of substrate molecules
37
How does the lock and key model explain denaturation?
Breaking of peptide bonds within the structure
38
What is the induced fit model?
Substrate and active site not entirely complimentary Can change shape - conformation When Substrate bonds with enzyme, induces change in enzymes conformation Active site moulded into precise conformation Bonds stretched to make reaction easier Chemical reaction is suitable
39
What factors effect enzymes?
Substrate concentration Ph Temperature Inhibitors
40
What are competitive inhibitors?
Structurally similar to substrate Blocks active site Cannot react with enzyme
41
What are non competitive inhibitors?
No structural similarity to substrate Binds to site other than active site Binding changes shape of active site
42
How does substrate concentration effect enzymes?
. Faster reaction until it reaches saturation point when enzyme molecules are occupied . If you alter concentration of enzyme then Vmax will change too
43
How does pH effect enzymes?
Extreme pH can produce denaturation Structure of enzyme changed Active site distorted Is pH values are slightly different from optimum small changes to enzyme and substrate occur Change in ionisation effects binding
44
How does temperature effect enzymes?
Enzymes are not denatured at cold temperatures As temperatures increase, substrate and enzyme have more kinetic energy High temperatures cause denaturation Changed due to excessive movement within the enzyme and the ionic and hydrogen bonds break Substrate will no longer fit