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3.1 Biological Molecules - Coggle Diagram
3.1 Biological Molecules
Carbohydrates
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Starch
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Amylopectin
1,4 and 1,6 glycosidic bonds
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Glycogen
1,4 and 1,6 glycosidic bonds
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Glucose + Glucose = maltose, Glucose + Fructose = sucrose, Glucose + Lactose = Galactose
Peptides
Structure
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Secondary - folding to stabilise structure with hydrogen bonds in alpha helicies and beta pleated sheets
Teritiery - further folding and securing of structure with hydrogen, disulphuric, ionic bonds
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E.g. Hormones, Antibodies, Enzymes
Lipids
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Phospholipids
Contain 1 phosphate, 1 glycerol and 3 fatty acids joined together with ester and phosphdioester bonds
Fatty acid tail is non-polar, phosphate head is polar
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ATP
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Made of Adenine, 3 phosphates
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Enzymes
Inhibitors
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Uncompetitive - bind to allosteric site and changes tertiary structure and shape of active site. This prevents the substrate from binding to it.
Factors affecting
Temperature - a higher temperature causes more kinetic energy. This cause the substrate and enzymes to move more and increase the chance of forming enzyme-substrate complexes.
Concentration - a higher concentration of substrates and/or enzymes increases the chance of forming enzyme-substrate complexes
pH - the amount of hydrogen and hydroxide ions have an affect on the hydrogen and ionic bonds in the enzyme changing its teitery structure and shape
Induced fit model
When the enzyme and substrate collide the enzyme moulds round the substrate. This stretches the bonds in the substrate meaning a lower activation energy can be used in the chemical reaction.
Bonds
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Hydrogen - electrons in molecule are not evenly distributed but tend to spend more time in one position. This becomes more negatively charged. The negative and positive regions of molecules attract forming an electrostatic bond.