Question

There are 20100 different possible sequence combinations for a protein chain with 100 amino acids. In addition to the amino acid sequence of the protein, what other factors increase the potential for diversity in these macromolecules?

(a) free rotation around single bonds during synthesis
(b) noncovalent interactions sampled as protein folds
(c) the directionality of amino acids being added
(d) the planar nature of the peptide bond

Answer 1

Protein diversity is influenced by factors such as noncovalent interactions as the protein folds, the directionality of amino acid addition, and the formation of quaternary structures from multiple polypeptides. These aspects, along with the planar nature of peptide bonds and the role of chaperone proteins, contribute to a protein's unique three-dimensional structure and function.

Step-by-step explanation:

The potential for diversity in protein macromolecules extends beyond the amino acid sequence, including factors such as:

• Noncovalent interactions that occur as the protein folds during and after synthesis, contributing to the formation of secondary and tertiary structures.
• The directionality in which amino acids are added, with the N-terminal amino acid written first and the C-terminal amino acid at the end, influencing the folding and function of the protein.
• Quaternary structures that result from the combination of multiple polypeptides, adding another level of complexity and diversity to protein structures.

Folding into complex three-dimensional shapes is determined by interactions among amino acid side chains and is facilitated by other proteins called chaperones. These shapes are crucial for the protein's function. Additionally, peptide bonds add to this complexity as they restrict rotation, influencing the final structure.