Answer:
1. Ser and Gln are polar amino acids.
2. The Leu side chain does not form hydrogen bonds with other amino acids.
3. Phe can undergo oxidation to form Tyr.
4. Lysine has one stereocenter (chiral center).
Explanation:
Serine and glutamine are the polar amino acids with uncharged side group. Serine has a "CH2OH" group as its side chain and the presence of hydroxyl group makes it a polar amino acid. Glutamine is one of the amides derived from other amino acids present in proteins.
Leucine is a nonpolar amino acid with an aliphatic side chain and tends to cluster within the proteins to stay away from the surrounding watery medium. Its aliphatic R group does not form any hydrogen bonds to other amino acids.
Phenylalanine is a nonpolar amino acid with an aromatic R group. Oxidation of aromatic R group of phenylalanine converts it into tyrosine which has an additional hydroxyl group in its side chain.
The chiral center is the carbon to which four different functional groups are bonded. The central alpha carbon atom of lysine is bonded to an amino group, carboxyl group, a hydrogen atom, and one positively charged R group which in turn makes it a chiral center.
Pea Plants--
The genetic experiments Mendel did with ( pea plants) took him 8 years (1856-1863) and he published his results in 1865. During this time, Mendel grew over 10,000 pea plants, keeping track of progeny number and types. Mendel's work and his laws of inheritance were not appropriated in his time.
A population of squirrels is preyed on by small hawks at maturity. the smaller adult squirrels can escape into burrows. the larger adult squirrels can fight off the hawks. after several generations, the squirrels in the area tend to be very small or very large. this is an example of disruptive selection. In disruptive selection, the extreme traits i.e., very small and very large sizes are favoured over intermediate trait i.e., average size.
The general term used for the special class of proteins that help other proteins to adopt their final fold structure is chaperones.
<h3>What are chaperones?</h3>
In proteomics, the term chaperones is used to denote a special class of proteins that serve to fol protein in the order they adopt the final tridimensional (3D) structure.
In conclusion, the general term used for the special class of proteins that help other proteins to adopt their final fold structure is chaperones.
Learn more about chaperone proteins here:
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