Answer
Randomly linking together amino acids typically are going to generate an insoluble polypeptide due to presence of higher number of hydrophobic amino acids with nonpolar moieties whereas a naturally occurring polypeptide (ex. globular proteins) of the same length is usually more soluble in aqueous solutions because of presence of high hydrophillicity & polar moieties. In the above given argument, it has not given, in which solutions these peptides are soluble or insoluble. However, randomly linking together amino acid is going to produce insoluble polypeptide due to presence of smaller side chains with lesser reactive functional groups in the aqueous solutions. Naturally occurring polypeptide of same length is usually soluble in aqueous solution due to presence of large amino acid side chains with reactive functional groups. These amino acid interactions in these polypeptides are both polar & nonpolar in nature to make them to fold with spherical conformations in aqueous solution.
Work Step by Step
Randomly linking together amino acids typically are going to generate an insoluble polypeptide due to presence of higher number of hydrophobic amino acids with nonpolar moieties whereas a naturally occurring polypeptide (ex. globular proteins) of the same length is usually more soluble in aqueous solutions because of presence of high hydrophillicity & polar moieties. In the above given argument, it has not given, in which solutions these peptides are soluble or insoluble. However, randomly linking together amino acid is going to produce insoluble polypeptide due to presence of smaller side chains with lesser reactive functional groups in the aqueous solutions. Naturally occurring polypeptide of same length is usually soluble in aqueous solution due to presence of large amino acid side chains with reactive functional groups. These amino acid interactions in these polypeptides are both polar & nonpolar in nature to make them to fold with spherical conformations in aqueous solution
