Answer:
Explanation:
A protease is an enzyme that catalyzes the hydrolysis of the peptide bonds that tie polypeptide chains together, releasing individual amino acid subunits. The L and D nomenclature for amino acids defines the structure of the glyceraldehyde isomer through which the amino acid can be produced.
SEE BELOW FOR THE APPROPRIATE STRUCTURES.
We need to figure out why swine proteases hydrolyze L-amino acids but not D-amino acids in any way. we know that enzymatic catalysts act as polypeptides if you can recall. They must retain a very precise three-dimensional structure for a catalytic activity to occur. Substrates that do not quite match the required configuration at the active site will not be reacted to — this is a "lock and key" style.
The present exercise may be explained by the fact that the configuration and structure of D-amino acids prevent them from binding properly to the active site of the protease enzyme. Perhaps they're pointed in the wrong direction, or perhaps there happens to be missing electrical interaction that's needed to keep the substrate in position.
Nonetheless, L-amino acids, on the other hand, seem to have the right configurational aspects in the active site and are hydrolyzed.
This is the structure of DNA and nucleotide is the phosphate group with sugar (the pink one ) and base that are 4 different bases : A, T, C, G and between these bases we have hydrogen bonds and you can see that always it like : C≡G
A=T :))) i hope that helps :)))https://www.google.com/url?sa=i&rct=j&q=&esrc=s&source=images&cd=&cad=rja&uact=8&ved=0ahUKEwiawYOO7-...
Answer:
analogous
Explanation:
both a bats wing and a butterfly wing are there for the same reason, but they are not composed the same
The bulk of the heart rests on the side of the body. On the left side
Mitochondria provides energy for moving chromosomes