Topic 1 Flashcards
What are receptors
Proteins on the cell surface or interior will respond to the target cell as it has the right shape.
Hormones can only bind to cells with the correct receptor.
How is the structure of a protein determined?
By it’s the unique sequence of amino acids
What does haemoglobin do
transport oxygen and carbon dioxide in the blood
What is a primary structure
sequence of amino acids joined by peptide bonds
Describe the side chains
side chains of amino acids determine the type of interaction with other amino acids
what is a secondary structure
small regions within the polypeptide consisting of alpha-helix and beta-sheet formed by hydrogen bonding
What is a tertiary structure
Final 3D folded structure of the polypeptide.
folding and coiling due to interactions between amino side chains and surrounding water
What is a quaternary structure
interactions with another polypeptide (2 or more)
how is the sequence of amino acids determined
by the sequence of codons in the gene
when do sulphide bridges form
when two cysteine amino acids are opposite each other in the polypeptide chains. consists of a covalent bond which is very strong compared to other bonds in tertiary structure. sulphide bridges can happen within a polypeptide or join two together.
What is denaturation?
a structural change in a protein that results in the loss (usually permanently) of its biological properties = can no longer function. usually caused by two key conditions - temperature and pH
What are enzymes
Molecules that carry out biological reactions increasing the rate of chemical reactions in cells.
why is the 3D shape of an enzyme critical to it’s function
The active site of an enzyme recognises and binds a substrate, but the shape of the substrate and the shape of the active site must be complementary.
Describe the induced fit model of an enzyme
Catabolic/breakdown reaction
- upon binding the enzyme undergoes a conformational change (induced fit) lowering the activation energy of the reaction by stressing the bonds holding the substrate together
- products are released and the enzyme is free to catalase another reaction
Describe induced fit of enzyme-substrate binding
Anabolic reaction
Combine monosaccharides to form polysaccharides.
upon binding the enzyme-substrate complex creates a bond between the two substrates to produce the product.
What is activation energy
the energy required to initiate a chemical reaction
How do anabolic reactions lower the activation energy
by aligning the substrates so that the bonds can be more readily made to create the product
How do catabolic reactions lower the activation energy
by stressing the bonds holding the substrate together so that the substrate is more readily broken to form the products
How does temperature effect enzyme activity
LOW TEMPERATURE
enzyme is in a good state, the rate of reaction is too low to locate the substrate to allow for binding
OPTIMAL TEMPERATURE
molecular motion is more rapidly resulting in more successful collisions between enzyme and substrate resulting in more product being formed
HIGH TEMPERATURE
colliding too fast and the enzyme is denaturing.
How does pH effect enzyme activity
LOW PH
excess H+ ions. charges become positive resulting in repulsion.
OPTIMAL PH
charges are opposite allowing for the substrate molecules to be attracted to the enzymes active site.
HIGH PH
lack of H+ ions. charges between active site and substrate become negative resulting in repulsion.
What happens at non-optimal pH?
change in charges of amino acids can change the shape of the active site. the ionic bonds in the enzyme are broken leading to unfolding of the polypeptide.
How do competitive inhibitors effect enzyme activity?
the inhibtor is similar enough in shape to a substrate that it can bind to the active site and simple block the substrate from binding. the rate of reaction will slow down.
How do non competitive inhibitors effect enzyme activity?
inhibitor molecule binds to the enzyme at a location other than the active site. These inhibitors change the conformation of the enzyme as well as the enzyme’s active site, so the substrate is not able to bind.
How does concentration of reactions effect enzyme activity
the rate of reaction increases with increasing substrate concentration. eventually, the concentration will exceed the availability of active sites and the rate of reaction will plateau and remain constant.