1A - Biological Molecules Flashcards

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1
Q

What is a polymer

A

A large molecule composed of many monomers

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2
Q

What is a condensation reaction

A

A reaction in which a chemical bond is formed between two molecules and water is released

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3
Q

What is the reaction that breaks polymers and what happens?

A

Hydrolysis: Water is used to break the bond formed by a condensation reaction forming two monomers

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4
Q

Example of two monomers

A

amino acids

glucose

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5
Q

What does a nucleic acid look like?

A

Pentose sugar bonded to a base and a phosphate

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6
Q

What is a carbohydrate?

A

Substance only containing the elements hydrogen, carbon and oxygen

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7
Q

What is a glycosidic bond?

A

A bond formed between two monosaccharaides

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8
Q

What to two monosaccharides form?

A

A disaccharide

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9
Q

Example of a polysaccharide?

A

Starch

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10
Q

Describe a test to find out if a substance contains non-reducing sugars.

A

Benedicts

Add sample to test tube and add Benedicts reagent. Heat solution for a couple of minutes. If colour doesn’t change from blue then non-reducing sugars are present. Then heat a new sample with dilute HCl and add sodium hydrogen carbonate. If the sample stays blue then there are no reducing or non-reducing sugars present

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11
Q

Structure of starch

A
Polysaccharide
Long chains of alpha glucose(Amylose, amylopectin)
Coiled chain
Compact structure
Hydrogen bonds make it insoluble
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12
Q

Structure of cellulose

A

Long unbranched chains of beta glucose
Each monomer is rotated 180 degrees in relation to each other.
Chains run straight and parallel to each other
Hydrogen bonds between chains creating microfibrils

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13
Q

Structure of glycogen

A

Similar to starch but is more branched and has shorter chains.
Alpha glucose
Compact

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14
Q

Structure of triglyceride

A

3 fatty acids attached to glycerol back bone

Ester bond between fatty acids and glycerol

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15
Q

Triglycerides are insoluble.

T/F?

A

True

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16
Q

What is a saturated lipid

A

One that has no double carbon bonds

17
Q

Structure of a phospholipid

A

Similar to triglyceride but one fatty acid is replaced by a phosphate group

18
Q

What is the primary structure of proteins

A

The chain/sequence of amino acids

19
Q

What is the secondary structure of proteins

A

Spiralled primary structure or pleated sheets held by hydrogen bonds

20
Q

Tertiary structure of proteins

A

3D shape held by ionic bonds and disulphide bridges and hydrogen bonds

21
Q

Quaternary structure

A

More than one tertiary structure chain

22
Q

Describe a test to test for the presence of proteins

A

Buirete test

  1. Make solution alkaline by adding sodium hydroxide solution
  2. Add copper(ii) sulphate solution
  3. If proteins are present then the sample will turn purple if not will remain blue
23
Q

What is an enzyme?

A

A biological catalyst which speed up a reaction without being used up in the reaction.

24
Q

What is activation energy?

A

The energy required to start a reaction

25
Q

What do enzymes do to the activation energy?

A

Lower it which speed up the rate of reaction

26
Q

Describe the structure of an enzyme

A
  • Has an active site

- Which is specific to the substrate it will bind to

27
Q

When a substrate fits into an enzyme’s active site it forms a…..

A

Enzyme-substrate complex

28
Q

Name the two models of enzyme action and explain them.

A

Lock and key - The enzyme and substrate have a complementary shape.
Induced fit - Substrate has to be able to slightly change the active site and then fit onto it.

29
Q

If the tertiary structure of an enzyme is change it is said to have become….

A

denatured

30
Q

Factors that denature an enzyme

A

pH
temperature
mutations in genes

31
Q

Measuring the rate of reaction can be done in two ways:

A

How fast the product is made

How fast the substrate is broken down

32
Q

The effect of temperature in enzyme controlled reactions

A

Increasing temp means more kinetic energy and so molecules move faster which increases collisions. However at too high temperatures the vibrations in the enzyme break bonds holding the shape of the enzyme which changes the active site and so it becomes denatured.

33
Q

pH

A

Above and below the optimum pH value ionic and hydrogen bonds are disrupted by H+ and OH- ions which changes the active site and denatures the enzyme.

34
Q

Substrate concentration

A

Increasing this will increase rate of reaction up until a point where the substrate concentration > enzyme concentration. This is because at this point there are no more active site to catalyse the reaction and so add more make no difference.

35
Q

Enzyme concentration

A

Increasing this will increase the rate of reaction up until the point where there is more enzymes than substrate.

36
Q

Describe the differences between competitive and non-competitive inhibitors.

A

Competitive - Have a similar shape to the substrate and so bind to the active site of the enzyme instead of the substrate.
Non-competitive - Bind to other parts of the enzyme other than the active site and cause a change in the shape of the active site.