B3b Flashcards
What are some examples of proteins?
Collagen, insulin and haemoglobin
What are proteins made of?
Long chains of amino acids.
What are some functions of proteins?
Structural Proteins - are physically strong. E.g. collagen is a structural protein that strengthens connective tissues.
Hormones - used to carry messages around the body. E.g. insulin is a hormone released into the blood by the pancreas to regulate the blood sugar level.
Carrier Molecules - used to transport smaller molecules. E.g. haemoglobin binds to oxygen molecules and transports them around the body.
Enzymes - control cell reactions. As a biological catalyst, they reduce the need for high temperatures and we only have enzymes to speed up the useful chemical reactions in the body. Every different biological reaction has its own enzyme designed especially for it.
What does each protein have and what does it result in?
Its own number and sequence of amino acids, which results in differently shaped molecules, which have different functions.
What are enzymes?
Proteins.
Work best at a particular temperature - each enzyme has its own optimum temperature when the reaction goes fastest.
Enzymes act as biological catalysts - a catalyst is a substance that speeds up a reaction, without being changed or used up in the reaction itself.
What do the active sites in enzymes do?
An active site is the part where it joins on to the substrate to catalyse the reaction. The substrate is the chemical changed in the reaction and chemical reactions usually involve things being split apart or joined together.
What are some examples of chemical reactions in living cells that are catalysed in enzymes?
Respiration, photosynthesis and protein synthesis.
Why do enzymes have a high specificity for their substrate?
Enzymes are really picky - they usually only work with one substrate.
What is the lock and key mechanism?
For enzymes to work, the substrate has to fit into the active site. If the substrate’s shape doesn’t match the active site’s shape, then the reaction won’t be catalysed . This is called the lock and key mechanism, because the substrate fits into the enzyme just like a key into a lock.
How will changing temperature and pH, away from the optimum, change the rate of reaction of an enzyme catalysed reaction?
If it gets too hot, some of the bonds holding the enzyme together will break. This makes the enzyme lose its shape - it’s active site doesn’t fit the shape of the substrate any more. This means it can’t catalyse the reaction and the reaction stops - the enzyme can’t function. The enzyme is now said to be denatured. Its change in shape is irreversible.
Low temperatures lower the collision rate so their is a slower reaction.
If the pH is too high or low, it interferes with the bonds holding the enzyme together. This changes the shape of the active site and denatures the enzyme.
Where is the optimum temperature and pH?
Each enzyme has its own optimum temperature when the reaction goes fastest. This is the temperature just before it gets too hot and starts to denature.
All enzymes have an optimum pH that they work best at. It’s often neutral pH 7, but not always.
How do you calculate the Q10 value for a reaction?
Q10 = rate at higher temperature/rate at lower temperature
It is for when the temperature is raised by 10 degrees C. e.g. using the rate between 30 and 40 degrees C.
How do you interpret the Q10 value?
The q10 value for a reaction shows how much the rate changes when the temperature is raised by 10 degrees C.
A Q10 value of 2 means that the rate doubles when the temperature is raised by 10 degrees C. A Q10 value of 3 would mean that the rate trebles.
What will different cells and different organisms produce?
Different proteins.
What are gene mutations?
Changes to genes.