1.3- Explain how changes in microscope technology, including electron microscopy, have enabled us to see cell structures and organelles with more clarity and detail than in the past and increased our understanding of the role of sub-cellular structures- light microscope
the light microscope was invented at the end of the 16th century and was used by Robert Hooke to discover cells in 1665. it had a magnification of x30 and resolution of 0.002. It was not very powerful.
The electron microscope was invented in the 1930s. Instead of light they passed beams of electrons through a specimen to build up an image. They had better detail and clarity because the magnification was up to x2000000 and resolution down to 0.0000002mm
1.6 Core Practical: Investigate biological specimens using microscopes, including magnification calculations and labelled scientific drawings from observation
add a drop of water or stain to microscope slide
place specimen on this
use a toothpick to slowly lower coverslip onto the specimen (means slide is less likely to contain air bubbles)
coverslip keeps the specimen flat, holds it in place and stops it from drying out
1.7- explain the mechanism of enzyme action including enzyme specificity
Different substrate have different 3D shapes, and different enzymes have different active site shapes. This explains why every enzyme can only work with specific substrates that fit the active site
1.8- explain how enzymes can be denatured due to changes in the shape of the active site
If the shape of the active site changes too much, the substrate will no longer fit in. The enzyme will no longer be able to catalyse a reaction, so the enzyme is denatured.
1.9- explain the effects of temperature, substrate concentration and pH on enzyme activity- temperature increasing
as the temperature increases, molecules move faster. higher speeds increase the chance of substrate molecules bumping into enzyme molecules and slotting into the active site.
However, when the temperature gets too high, the shape of the enzyme molecule starts to change (denature) . the amount of change increases as the temperature increases. so it becomes more difficult for a substrate molecule to fit into the active site
at low concentrations, many enzyme molecules have empty active sites so the rate of reaction is slow. At high concentrations, most enzyme active sites contain substrate molecules, and the rate of reaction is as fast as it can be
the optimum pH is 7 (neutral). At pHs above and below the optimum, the shape of the active site is affected (denatured) and so the enzyme does not work as well.
1.10- core practical: investigate the effect of pH on enzyme activity
heat water to 40 degrees. Place one drop of iodine solution into each dimple tile. Measure 2cm cubed of amylase solution into a tube. add 1mc cubed of a solution with a particular pH into the tube. Add 2cm cubed of starch solution to the tube and place it carefully into the water bath. start stop clock and stir. Every 20s, take a small amount of mixture and place one drop into a fresh iodine solution. stop testing when iodine solution stops changing colour. repeat with different pHs
1.12- explain the importance of enzymes as biological catalysts in the synthesis of carbohydrates, proteins and lipids and their breakdown into sugars, amino acids and fatty acids and glycerol- importance
digestive enzymes turn the large molecules in our food into the smaller subunits they are made of. the digested molecules are then small enough to be absorbed by the small intestine