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.
Answer:
Diarthroses are freely movable joints.
Explanation:
Rheumatology may be defined as the branch of medicine that mainly deals with therapy and diagnosis of the rheumatic disease. The individual specialized in this field is known as rheumatologist.
Diarthroses joint is also known as synovial joint and lined in continuous with the periosteum of the joined bones. The synovial fluid is filled in the synovial joint. The synovial joints provide the free movable joints that allow abduction, extension and adduction of the body parts.
Thus, the correct answer is option (d).