Biological Molecules Flashcards

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0
Q

Explain the polarity of water.

A

The shared hydrogen and oxygen electrons are pulled towards the oxygen atom. Hydrogen is left with a slight positive charge and oxygen has a slight negative charge. Making it a polar molecule.

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1
Q

What are the key functions of water?

A

Reactant is important chemical reactions
Helps transport substances - good solvent and cohesive
Temperature control - high specific heat capacity and high latent heat of evaporation
Good habitat because it has a high specific heat capacity, less dense when it freezes.

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2
Q

Explain why hydrogen bonding occurs in water.

A

Hydrogen bonds occur between the slightly positively charged hydrogen atom and slight negatively charged atom in another molecule. This happens in water because hydrogen is slightly positive and oxygen is slightly negative - causing an attraction.

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3
Q

Why does water have a high specific heat capacity and why does this help organisms?

A

A lot of energy is required to break of the bonds between the molecules, there is less energy left over to raise the temperature of the water. This is useful for temperature stability.

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4
Q

Why does water have a high latent heat of evaporation and why is this useful?

A

A lot of energy is required to break the bonds between water, so a lot of energy is needed when water evaporates. Changing state from liquid to a gas requires a lot of energy. Therefore giving it a high latent heat of evaporation. Great for cooling things as it takes a lot of heat away.

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5
Q

Why is water so cohesive and why is this useful?

A

They are very cohesive because water molecules are so polar. This makes them great for transporting substances.

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6
Q

Why does water have a lower density when solid and why is this useful?

A

Water molecules are held further apart when they are solid as the hydrogen bonds elongate. Making it less dense. This forms an insulating layer as ice floats to the top. So organisms below don’t freeze.

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7
Q

Why is water a good solvent and why is this useful?

A

ionic compounds are most important for biology. Water is slightly positively charged and slightly negatively charged. Ions will surround why water molecules. Therefore dissolves. This is good for transporting substances in blood, xylem, phloem etc…

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8
Q

Proteins are made up of…

A

Polypeptide chains

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9
Q

Two amino acids form…

A

Dipeptide

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10
Q

Two or more amino acids form…

A

Polypeptide chains

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11
Q

Name the different parts of an amino acids

A

R variable group, carboxyl group and amino group.

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12
Q

Peptide bonds are formed by which reaction?

A

Condensation reaction.

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13
Q

Peptide bonds are broken by…

A

Hydrolysis reactions (addition of water)

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14
Q

What is the primary structure of a protein?

A

It is the sequence of amino acids that are determined by the gene that they are coded for by.

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15
Q

What is the secondary structure?

A

Hydrogen bonds form between the -NH and -CO groups between chains of amino acids. This makes them coil and fold into alpha helices and beta pleated sheets.

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16
Q

What is the tertiary structure?

A

It is determined by many different bonds related to the r groups on amino acids in polypeptide chains.
Ionic interactions - weak attractions between negatively charged r groups and positively charged r groups on different parts of the molecule.
Disulphide bonds - whenever two molecules of cysteine come close the sulphur atoms in their r groups form Disulphide bonds. Or other sulphur containing r groups. They are covalent bonds.
Hydrophobic and hydrophilic interactions - when hydrophobic r groups and close together they clump together and hydrophilic r groups and pushed onto the outside. Affecting how the protein folds.
Hydrogen bonds - weak bonds between slight positive charge of a hydrogen atom in one r group and slightly negative charged atoms in other r groups on polypeptide chains.

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17
Q

Explain 3 difference between globular and fibrous proteins.

A

Globular proteins role to form balls, where as fibrous form fibres. Globular are soluble in water where as fibrous aren’t. Globular form metabolic functions where as fibrous have structural roles.

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18
Q

Describe the structure of haemoglobin

A

It is a globular protein. It is soluble in water because the hydrophilic r groups are on the outside and hydrophobic are on the inside. Wide range of amino acid constituents. Each polypeptide chain has its on haem group (Fe2+ that binds to the oxygen). Made up of two alpha chains and two beta chains. Most of the structure is alpha helices.

19
Q

Describe the structure of collagen

A

Made up of three polypeptide chains consisting mainly of glycine (35%). Forms cross links between the chains which are covalent bonds. It is insoluble in water. No prosthetic group. Consists of left handed helices. Fibrous protein.

20
Q

What are the difference between collagen and haemoglobin?

A

Haemoglobin soluble in water, collagen isn’t. Haemoglobin is globular protein where as, collagen is a a fibrous protein. Collagen is made up of mainly left hand helices where as haemoglobin is made of alpha helices. Haemoglobin four polypeptide chains two alpha and two beta each with an fe2+ haem group! collagen is made up three polypeptide chains. Haemoglobin has a wide range of amino acid constituents where as collagen has 35% glycine.

21
Q

Why is collagen and cellulose similar?

A

Both are fibrous, giving rigid structure to support organisms. Molecule fibres are strengthened by bundling together. Multiple hydrogen bonds are responsible for holding the bundles of fibres together.

22
Q

What are the monomers of carbohydrates?

A

Monosaccharides.

23
Q

How are polysaccharides joined together?

A

Glycosidic bonds

24
Q

How do alpha and beta glucose differ?

A

The OH is above on the beta and below on the alpha

25
Q

What type of glycosidic bonds are alpha glucose joined by.

A

1,4 glycosidic bonds

26
Q

What are the two constituents of starch?

A

Amylose and amylopectin.

27
Q

Describe the structure of amylose and why is it useful.

A

It is a long unbranched chain of alpha glucose. The bonds between two alpha glucose differ than they are between two beta glucose molecules. This gives it a coil structure, almost like a cylinder. Make it good for storage.

28
Q

Describe the structure of amylopectin and why is it useful.

A

It is long branched chain of alpha glucose. The side chains allow the enzyme to break down the molecule and made it easier to break the glycosidic bonds. Energy can be released more quickly.

29
Q

Describe the structure of glycogen and why is it useful

A

The 1,4 glycosidic bonds are much shorter in glycogen and the chain is much more branched, making it more compact than starch. Important for energy release.

30
Q

What is similar between all of these energy storage molecules.

A

They aren’t soluble so doesn’t affect water potential.

Chains are easily broken off.

31
Q

Describe the structure of cellulose and why it is useful.

A

Made up of repeating units of long unbranched chains of beta glucose. Bonds are straight, cellulose chains are straight. Linked together by hydrogen bonds to form strong fibre called microfibrils. This makes it good for structural support.

32
Q

Describe the structure of a triglyceride.

A

One molecule of glycerol attached to three fatty acid tails. Bonded by ester bonds.

33
Q

Structure of a fatty acid tail

A

Carboxyl group with r group of a varying length of hydrocarbon attached to it

34
Q

Difference between saturated and unsaturated fatty acid tails.

A

Saturated have only single bonds where as, unsaturated have double bonds.

35
Q

Structure of phospholipid.

A

Glycerol with a phosphate group at top and two fatty acid tails below.

36
Q

Structure of cholesterol.

A

Hydrocarbon ring structure with attached polar hydroxyl group. On other side has attached hydrocarbon tail.

37
Q

Function of triglycerides and how they are adapted

A

Mainly used as storage molecules. Good because they are used as they have long hydrocarbon tails with lots of energy. Also insoluble in water so don’t affect the water potential in cells.

38
Q

Functions of phospholipid and how it is adapted.

A

Form bilayer of cell membranes. Phosphate head hydrophilic and tails are hydrophobic. Tails face inwards, the form a hydrophobic centre which makes it hard for water soluble substances to enter.

39
Q

Functions of cholesterol and how it is adapted.

A

The strengthen the cell wall (making it less fluid and more rigid) by interacting with the bilayer. They are small so slot in between the phospholipid tails. This causes them to pack closer together.

40
Q

How to carry out a test for proteins and describe a positive test result.

A

Solution must be alkaline so add sodium hydroxide and then add copper (II) sulfate. Positive test is blue to purple

41
Q

Test for reducing sugar and what would the results look like?

A

Add Benedict’s solution and then heat it. Green to yellow to orange to red.

42
Q

Test for non reducing sugar and results

A

Boil in HCl and then add sodium hydrocarbonate to neutralise. Add Benedict’s then heat it. Green to yellow to orange to red.

43
Q

What is a colorimeter?

A

An apparatus that measures the strengthen of a coloured solution by measuring the absorbance.

44
Q

How to make a calibration curve

A

Make glucose solutions of known compounds at different concentrations. Put it in excess Benedict’s reagent. Remove precipitate and let it settle for twenty four hours. Use colorimeter to measure the absorbance. Use colorimeter with red filter. Put results on a calibration curve.

45
Q

What is the test for starch and positive results?

A

Iodine in dissolved potassium iodide. From browny orange to blue-black.

46
Q

Test for lipids and positive results.

A

Put the substance with ethanol then shake it. Then pour into water. If there is a cloudy solution at the top, there are lipids.