BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions.

Detailed explanation-2: -The tertiary structure is primarily due to interactions between the R groups of the amino acids that make up the protein.

Detailed explanation-3: -The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space. It is generally stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between nonpolar amino acid side chains (Fig.

Detailed explanation-4: -Primarily, the interactions among R groups creates the complex three-dimensional tertiary structure of a protein. The nature of the R groups found in the amino acids involved can counteract the formation of the hydrogen bonds described for standard secondary structures.

Detailed explanation-5: -The hydrophobic effect leads to the burial of nonpolar side chains in the interior of proteins, which in turn collapses polypeptide chains into compact, globular structures. This collapse does not, however, happen because van der Waals interactions in the interior are favorable (they are but only weakly so).