Entropy, is mainly responsible for the resting state of this protein.
Hydrogen bonds, disulfide bonds, and dipole-dipole interactions produce the complicated folding styles seen in secondary and tertiary structure. however, if a protein does not have these elements of structure, it'll undertake a kingdom in which its entropy is maximized.
Secondary shape is determined through hydrogen bonding within the amino acid chain backbone. Tertiary structure is the entire protein's form, decided Entropy Interplay and hydrophobic forces. The tertiary shape of a protein is the 3 dimensional shape of the protein. Disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions all affect the form a protein takes.
The nonpolar amino acids have formed the nonpolar center of the protein, weak van der Waals forces stabilize the protein. furthermore, hydrogen bonds and ionic interactions between the polar, charged amino acids make a contribution to the tertiary structure.
Disclaimer: your question is incomplete, please see below for complete question
A. Entropy
B. Hydrogen bonds between amino acid residues
C. Dipole-dipole interactions
D. None of the above
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