The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
it might be a protein.. since proteins are polymers of various amino acids..
i dont know it.!
point mutations include substitutions insertions and deletions of a single nuceotide in DNA. CONSIDER: insertions and deletions have a greater effect on proteins that do substiutions because insertions and deletions affect every amino acid that is specified by the nucleotides that follow the point of mutation CONSIDER: a substitution affects a single amino acid a change in more than one amino acid is more likely to alter the ability of the protein to function narmally than is a change in a single amino acid CONSIDER: follow me on twitter @Rocco_Gone_Ham
An enzyme can lose its shape (tertiary structure) through many ways. Some of these include: pH change, increased heat, or change in ionic strength of the solution (increasing or decreasing salt levels).
The sequence of nucleotides is altered and therefore, the amino acid that is to be added to the peptide chain will be altered. hence the protein will be different. This protein can be functionless (will be degraded). If it turns out to be toxic, then there may be symptoms.
The alteration of an amino acid on a site other than the active site will: change the shape of the protein.
it might be a protein.. since proteins are polymers of various amino acids..
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
i dont know it.!
point mutations include substitutions insertions and deletions of a single nuceotide in DNA. CONSIDER: insertions and deletions have a greater effect on proteins that do substiutions because insertions and deletions affect every amino acid that is specified by the nucleotides that follow the point of mutation CONSIDER: a substitution affects a single amino acid a change in more than one amino acid is more likely to alter the ability of the protein to function narmally than is a change in a single amino acid CONSIDER: follow me on twitter @Rocco_Gone_Ham
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
Enzymes are quite easy to break.So if the pH is too acidic,then the enzyme might break.Therefore if the temperature is too high,the enzyme will also break.
The proteins in the amino-acids might have been responsible for the change in the hemoglobin between gorillas and humans.
A mutation is a change in DNA, so when u change the DNA this affects the sequence of the amino acid in the primary structure. this later changes the folding of the r groups because u don't have the right unique sequence of amino acid that was encoded by the DNA
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
It will depend on how different the amino acid is to the one it replaced. If the structure and/or charge is quite different, a change of one amino acid can change the entire 3D structure of the protein. This will affect the proteins function.
An enzyme can lose its shape (tertiary structure) through many ways. Some of these include: pH change, increased heat, or change in ionic strength of the solution (increasing or decreasing salt levels).