Final answer:
The sequence alanine-glycine-leucine is most likely to be found in the inner core of a cytosolic protein, due to the nonpolar, hydrophobic nature of its amino acids. This matches the characteristics required for stability within the protein's inner core.
Step-by-step explanation:
The question focuses on predicting which tripeptide sequence would be found in the core of a cytosolic protein. Considering the nonpolar, hydrophobic nature of the inner core of proteins to stabilize their structure, we can identify the most likely amino acid sequence for this environment. Tripeptides are short chains of three amino acids connected by peptide bonds, and the sequence matters immensely as it determines the properties of the peptide.
The primary structure of proteins is the unique sequence of amino acids in a polypeptide chain, dictated by the genetic code. It is linear and defines the fundamental structure of the protein. Amino acids in a tripeptide are written from the N-terminus, which has a free amine group, to the C-terminus, with a free carboxyl group, such as in the tripeptide Gly-His-Lys.
Among the given options, sequence B) alanine-glycine-leucine consists of amino acids with nonpolar, hydrophobic side chains, making it the most likely to be found in the inner core of a cytosolic protein. In contrast, the other sequences contain polar or charged amino acids, which are typically found on the surface of proteins, interacting with the aqueous cellular environment.