<span>Obesity acts as an important risk factor for type 2 diabetes mellitus by
</span>
Answer;
-Serous membrane
Explanation;
-Serous membranes are thin membranes that lines the internal body cavities and organs such as the heart, lungs, and abdominal cavity. The thin membrane is made up of mesothelium tissue which originates from the mesoderm.
-These membranes consists of a single layer of flattened mesothelial cells applied to the surface of a thin layer of collagenous tissue that attaches to underlying endothoracic/transversalis fascia. They function to preclude adhesions among organs, thereby allowing organs to move freely relative to one another.
The answer is
D) Pp, PP, and pp.
i attached a picture of a punnett square i did to help you understand the answer more, if you want.
1. Two genetically identical copies of DNA
2. Finds an error in DNA, removes the incorrect nucleotide and replaces it with a correct one.
3. It is used as a copy/ "template" for replication in order to have two identical copies of DNA.
4. DNA helicase unwinds DNA double helix and Topiosomerase ensure there isn't too much unwinding.
5. Replication has a built on proofreading system - DNA polymerase removes the incorrect nucleotide and replaces it with a correct one.
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.