1 Biological molecules

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  • Created by: sydjow17
  • Created on: 02-12-19 10:30
Define monomers.
The smaller units from which larger molecules are made.
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Define polymers.
Molecules made from a large number of monomers joined together.
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What is a condensation reaction?
A reaction that joins two molecules together with the formation of a chemical bond, and involves the elimination of a molecule of water.
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What is a hydrolysis reaction?
A reaction that breaks a chemical bond between two molecules, and involves the use of a water molecule.
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Define monosaccharides and give some examples.
The monomers from which larger carbohydrates are made, e.g. glucose, galactose and fructose.
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Describe the formation of a disaccharide, and give some examples.
Formed by the condensation reaction of two monosaccharides, forming a glycosidic bond between the two, e.g. maltose, sucrose and lactose.
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Define metabolism.
All the chemical processes that take place in living organisms collectively.
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Define molar solution.
A solution that contains one mole of solute in each litre of solution (mol/dm^3)
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Describe the formation of a triglyceride.
They have three fatty acids combined with one glycerol molecule, with each fatty acid forming an ester bond with glycerol in a condensation reaction.
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What is the difference between saturated and unsaturated fatty acids?
A fatty acid is saturated when all the carbon atoms are linked to the maximum possible number of hydrogen atoms; unsaturated fatty acids contain one or more double bonds.
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How does the presence of double bonds affect the physical properties of fatty acids?
The double bonds cause the molecule to bend. They cannot therefore pack together so closely making them liquid at room temperature, i.e. they are oils.
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How are phospholipids different to lipids?
One of the fatty acids is replaced by a phosphate molecule, which makes the phospholipid polar.
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Describe the two parts which make up a phospholipid.
S hydrophilic phosphate head and a hydrophobic tail of two fatty acids.
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Summarise the general structure of an amino acid.
A central carbon atom to which four different chemical groups are attached; these are an amino group, a carboxyl group, a hydrogen atom, and an R (side) group.
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Define amino acid.
The monomers from which proteins are made.
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Describe the formation of a peptide bond.
A condensation reaction between two amino acids forming peptide joined by a peptide bond.
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How is the water made in the condensation reaction between two amino acids.
By combining an -OH from the carboxyl group of one amino acid with an -H from the amino group of another.
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Describe the primary structure of a protein.
The sequence of amino acids in a polypeptide chain.
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Describe the secondary structure of a protein.
Hydrogen bonding causes the long polypeptide chain to be twisted into a 3D shape, such as a coil known as an alpha-helix.
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Describe the tertiary structure of a protein.
Due to the bending and twisting of the polypeptide helix into a compact structure. This structure is maintained by a number of different bonds; including disulfide bridges, ionic bonds and hydrogen bonds.
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Describe the quaternary structure of a protein.
Arises from the combination of a number of different polypeptide chains and associated prosthetic (non-protein) groups into a large, complex protein molecule.
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Define enzyme.
Enzymes are globular proteins that act as catalysts, by lowering the activation energy of the reaction it catalyses.
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Describe the enzyme-substrate complex.
The substrate molecule is held within the depression of the enzyme that is the active site, by bonds that temporarily form between certain amino acids of the active site and groups on the substrate molecule.
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Describe the induced fit model of enzyme action.
Proposes that the active site forms as the enzyme and substrate interact. The proximity of the substrate leads to a change in the enzyme that forms the functional active site.
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How do enzymes lower activation energy?
The enzyme puts a strain on the substrate molecule, which distorts a particular bond or bonds in the substrate and consequently lowers the activation energy needed to break the bond.
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How can you measure the progress of an enzyme-catalysed reaction?
Measure the formation of the products of the reaction, or the disappearance of the substrate.
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Define enzyme inhibitor.
Substances that directly or indirectly interfere with the functioning of the active site of an enzyme and so reduce its activity.
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Define competitive inhibitors.
A type of enzyme inhibitor which binds directly to the active site of the enzyme.
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Define non-competitive inhibitors.
A type of enzyme inhibitor which binds to the enzyme at a position other than the active site.
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Other cards in this set

Card 2

Front

Define polymers.

Back

Molecules made from a large number of monomers joined together.

Card 3

Front

What is a condensation reaction?

Back

Preview of the front of card 3

Card 4

Front

What is a hydrolysis reaction?

Back

Preview of the front of card 4

Card 5

Front

Define monosaccharides and give some examples.

Back

Preview of the front of card 5
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