Griffith's experiment worked with two types of pneumococcal bacteria (a rough type and a smooth type) and identified that a "transforming principle" could transform them from one type to another.
At first, bacteriologists suspected the transforming factor was a protein. The "transforming principle" could be precipitated with alcohol, which showed that it was not a carbohydrate. But Avery and McCarty observed that proteases (enzymes that degrade proteins) did not destroy the transforming principle. Neither did lipases (enzymes that digest lipids). Later they found that the transforming substance was made of nucleic acids but ribonuclease (which digests RNA) did not inactivate the substance. By this method, they were able to obtain small amounts of highly purified transforming principle, which they could then analyze through other tests to determine its identity, which corresponded to DNA.
Just as animals, plants also contain vascular<span> tissues (</span>xylem<span>), which transports water and minerals up from the roots to the leaves, and </span>phloem<span>, which transports sugar molecules, amino acids, and hormones both up and down through the plant</span>
Answer:
A few obstacles would make it tough to accomplish this objective. In the first place, the polypeptide backbone is characteristically polar. Hardly any proteins would be dissolvable in a non-polar hydrocarbon. Moreover, to keep up the dissolvability of this protein, most of its amino acids would need to contain hydrophobic or non-polar R groups.
Then again, its charged or polar R groups would need to connect with one another or be covered in the core of the protein away from the hydrocarbon solvent. This would put noteworthy requirements on both the idea of the R groups and the structure of the protein that could take part in substrate recognition or catalysis. By and large, this is certainly not a reasonable objective.
