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Biology A level > Biological molecules - Yr 1 > Flashcards

Biological molecules - Yr 1 Flashcards

1
Q

Name 4 types of biological molecule

A 
Carbohydrates
Proteins
Lipids
Nucleic acids
(water)
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2
Q

What elements are found in carbohydrates?

A

Carbon, Oxygen and Hydrogen

C, O & H

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3
Q

What elements are found in lipids?

A

Carbon, Hydrogen and Oxygen

C, H, O

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4
Q

What elements are found in the basic amino acid?

A

Carbon, Oxygen, Hydrogen, Nitrogen

(many other elements can be found in the functional R-Group of the amino acids

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5
Q

What two molecules make up starch

A

Amylose and amylopectin

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6
Q

What glycosidic bonds are found in amylose?

A

1,4 glycosidic bonds

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7
Q

What glycosidic bonds are found in amylopectin?

A

1,4 AND 1,6 glycosidic bonds

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8
Q

Draw alpha glucose

A

Image here

http://www.robertbarrington.net/alpha-glucose/

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9
Q

Draw Fructose

A

Image here:

https://en.wikipedia.org/wiki/Fructose_malabsorption

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10
Q

Draw maltose

A

image here:

https://www.quora.com/How-does-maltose-and-starch-differ

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11
Q

What monomers make maltose?

A

Two alpha glucose

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12
Q

What monomers make up sucrose?

A

Fructose and glucose

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13
Q

What monomers make up lactose?

A

Glucose and galactose

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14
Q

What bone is formed between sugar monomers?

A

Glycosidic

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15
Q

What type of reaction adds monomers together in biological molecules

A

Condensation - water is given out as a product

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16
Q

What type of reaction splits monomers in biological molecules?

A

Hydrolysis - water is needed as a reactant to split the molecules

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17
Q

Draw a basic amino acid

A

image here:

https://en.wikibooks.org/wiki/Medical_Physiology/Basic_Biochemistry/Amino_Acids_and_Proteins

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18
Q

What bond forms between amino acids?

A

peptide

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19
Q

What names are given to proteins as they form greater levels of complexity?

A

Primary
Secondary
Tertiary
Quarternary

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20
Q

What is the primary structure of a protein

A

A single chain of amino acids

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21
Q

What is the secondary structure of a protein?

A

When hydrogen bonding has formed
Or di-suphide bridges
Often an alpha helix shape or a beta pleated sheet

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22
Q

What is the tertiary structure of a protein?

A

When the protein is fully folded, still one folded amino acid chain. It can incorporate other elements or molecules in it. Can be globular in shape (enzymes)

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23
Q

What is a quarternary protein?

A

This is a complete protein that is made from more than one amino added chain attached to one another. So multiple tertiary proteins attached to each other. Haemoglobin is an example of four tertiary proteins (each incorporating a Haem group (Iron)) all attached to one another

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24
Q

What are lipids made from?

A

Glycerol and fatty acids?

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25
Q

What is a triglyceride?

A

one glycerol with 3 Fatty Acids attached

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26
Q

What bond is formed in lipids?

A

Ester bonds

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27
Q

What gives triglycerides different properties?

A

The variation in the fatty acid chains

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28
Q

What can be different about the fatty acid chains?

A

they can be longer or shorter

they can contain no, single or multiple double bonds

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29
Q

What do double bonds between carbon atoms in fatty acid chains do to the property?

A

They put bends in the chain (kinks) this makes the final triglyceride less dense and more reactive in metabolism

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30
Q

What difference does the length of fatty acid chain make to the property of a triglyceride

A

the longer the chain the higher the melting point

eg Long chain fatty acids will be solid at room temperature

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31
Q

Covalent Bond

A

Type of chemical bond in which two atoms share a pair of electrons.

32
Q

Ionic Bond

A

A bond between a positive ion which has lost an electron(s) and a negative ion which has gained an electron(s).

33
Q

Hydrogen Bond

A

Chemical bond formed between the positive charge on a hydrogen atom and the negative charge on another atom of an adjacent molecule e.g. between the Hydrogen atom of one water molecule and the Oxygen atom of an adjacent water molecule

34
Q

Polar Molecule

A

A molecule which has a partially positive charge in one part of the molecule and completely negative charge in another part (a dipole).

35
Q

Monomer

A

One of many small molecules that combine together to form a polymer

36
Q

Polymer

A

Large molecule made up of many repeating smaller molecules (monomers).

37
Q

Polymerisation

A

The process of making a polymer

38
Q

Metabolism

A

All the chemical processes that take place in living organisms.

39
Q

Mole (chemical)

A

The mass of a substance containing the same number of fundamental units as there are atoms in exactly 12g of 12C.

40
Q

Monosaccharide

A

A single sugar e.g. glucose with no glycosiidic bond

41
Q

Disaccharide

A

Made up of two sugar units that are formed by a condensation reaction. Monosaccharides are joined by a glycosidic bond.

42
Q

Polysaccharide

A

Made of many sugar units that are formed by a condensation reaction. Monosaccharides are joined by a glycosidic bond.

43
Q

Hexose sugar

A

A sugar made up of 6 carbons.

44
Q

Reducing Sugar

A

A sugar that serves as a reducing agent. All monosaccharides are reducing sugars along with some disaccharides.

45
Q

Reducing sugar test

A

Heat solution with Benedict’s reagent to test for reducing sugars. If it goes brick red then a reducing sugar is present.

46
Q

Benedict’s reagent

A

Blue solution which is used to test for reducing and non-reducing sugars.

47
Q

Non-reducing sugar

A

A sugar which cannot serve as a reducing agent. An example is sucrose.

48
Q

Non-reducing sugar test

A

Following a negative reducing sugars test. Heat the solution with HCl to hydrolyse the non-reducing sugar into it’s monosaccharides. Then perform the Benedict’s test again. If you get a positive result after hydrolysis then a non-reducing sugar is present.

49
Q

Glycogen

A

A highly branched polysaccharide made up of alpha-glucose found in animal cells (alpha-1,4- and alpha-1,6-glyosidic bonds).

50
Q

Cellulose

A

A polysaccharide made up of beta-glucose found in plant cells (beta-1,4-glycosidic bonds).

51
Q

Saturated fatty acid

A

A fatty acid in which there are no double bonds between the carbon atoms

52
Q

Mono-unsaturated fatty acid

A

Fatty acid which possesses a carbon chain with a single double bond between carbon atoms.

53
Q

Poly-unsaturated fatty acid

A

Fatty acid which possesses a carbon chain with many double bonds between carbon atoms.

54
Q

Phospholipid

A

Triglyceride in which one of the three fatty acid molecules is replaced by a phosphate molecule. Phospholipids are important in the structure an functioning of plasma membranes.

55
Q

Hydrophilic

A

Section of a molecule which is attracted to water.

56
Q

Hydrophobic

A

Section of a molecule which is repulsed by water.

57
Q

Emulsion test

A

Test for lipids. Mix your sample with ethanol and then add water. If a white cloudy emulsion forms then a lipid is present.

58
Q

Amino group

A

The -NH2 group of an amino acid.

59
Q

Carboxyl group

A

The -COOH group of an amino acid.

60
Q

R-group

A

Each of the 20 amino acids has a different R group – determines the bonding that the amino acid can carry out.

61
Q

Polypeptide

A

Many amino acids joined together by peptide bonds.

62
Q

Biuret test

A

A simple biochemical reaction to detect the presence of protein, if the Biuret’s solution turns purple then protein is present.

63
Q

Enzyme

A

A protein that acts as a catalyst and so lowers the activation energy needed for a reaction.

64
Q

Activation energy

A

Energy required to bring about a reaction.

65
Q

Active Site

A

A group of amino acids that makes up the region of an enzyme into which the substrate fits in order to catalyse a reaction.

66
Q

Substrate

A

A substance that is acted on or used by another substance or process. Fits into the active site of an enzyme.

67
Q

Enzyme-substrate complex

A

The intermediate formed when a substrate molecule interacts with the active site of an enzyme.

68
Q

Complimentary

A

Describes the relationship between the active site of an enzyme and the substrate molecule – the way in which they fit together.

69
Q

Specific

A

Describes how enzymes catalyse a certain chemical reaction.

70
Q

Induced fit

A

A mechanism of interaction between an enzyme and a substrate. As the substrate fits into the active site the active site of the enzyme changes shape in order to allow an enzyme-substrate complex to be formed.

71
Q

Lock and key

A

An analogy for how enzymes work – only the correctly sized key (substrate) fits into the key hole (active site) of the lock (enzyme)

72
Q

Rate of reaction

A

The speed of a chemical reaction - can be worked out by looking at the decrease in concentration of a reactant over time or increase in concentration of a product over time.

73
Q

Kinetic Energy

A

The energy of motion, observable as the movement of an object, particle or set of particles.

74
Q

pH

A

A figure expressing the acidity or alkalinity of a solution on a logarithmic scale on which 7 is neutral, lower values are more acidic and higher values are more alkaline. Equivalent to -log10[H+].

75
Q

Inhibitor

A

A substance which reduces the activity of an enzyme.

76
Q

Competitive inhibitor

A

A form of inhibitor which binds to the active site of the enzyme preventing the binding of substrate.

77
Q

Non-competitive inhibitor

A

A form of inhibitor which does not bind at the active site of the enzyme which prevents the binding of substrate.

Biology A level (21 decks)

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