By starch, I'm assuming you mean glycogen, or animal starch.
Similarities:
Both are polysaccharide molecules made from glucose molecules linked together in a long chain.
Both are storehouses of energy.
Differences:
Glycogen is made in animal cells and is the only form of starch animals can digest (unless they have certain microbes in their intestinal tracts to break down cellulose, which all herbivores need).
Cellulose is made in plant cells.
The bonds are a bit different; the molecules are isomers. Glycogen bonds with what is called an alpha 1,4 bond, meaning that the first carbon of one glucose molecule is bonded to the 4th carbon of the next glucose molecule, but in a way that puts the bonds in a shape that falls below the plane of the molecule, and allows branching.
Cellulose bonds with beta 1,4 bonds. The first and fourth carbons of adjoining glucose molecules are still connected, but the shape of the bond falls above the plane of the molecule and does not branch.
Since enzymes are specific to their substrates, the enzymes shaped to fit glycogen bonds do not fit on cellulose bonds, which is why animals cannot digest cellulose on their own. In herbivores, there are microbes in their digestive tracts which can produce enzymes to break these bonds so the glucose can be used. In carnivores and omnivores like humans, there is no enzyme to break down cellulose so it becomes 'roughage' in our diets. It passes through the digestive tract without being broken down.
Capillaries are the end structures in the artery system that bring oxygenated blood from your lungs to the rest of your body.
B. stationary front it has high winds and leaves precipitation, warm front doesn't really have the strong winds.
Answer:
please mark as brainliest answer as it will also give you 3 points
Explanation:
Cyclin-dependent kinases (CDKs) are the families of protein kinases first discovered for their role in regulating the cell cycle. They are also involved in regulating transcription, mRNA processing, and the differentiation of nerve cells.[1] They are present in all known eukaryotes, and their regulatory function in the cell cycle has been evolutionarily conserved. In fact, yeast cells can proliferate normally when their CDK gene has been replaced with the homologous human gene.[1][2] CDKs are relatively small proteins, with molecular weights ranging from 34 to 40 kDa, and contain little more than the kinase domain.[1] By definition, a CDK binds a regulatory protein called a cyclin. Without cyclin, CDK has little kinase activity; only the cyclin-CDK complex is an active kinase but its activity can be typically further modulated by phosphorylation and other binding proteins, like p27. CDKs phosphorylate their substrates on serines and threonines, so they are serine-threonine kinases.[1] The consensus sequence for the phosphorylation site in the amino acid sequence of a CDK substrate is [S/T*]PX[K/R], where S/T* is the phosphorylated serine or threonine, P is proline, X is any amino acid, K is lysine, and R is arginine.[1]
