The correct answer is option 'C', peptide bonds.

Peptide bonds are the specific type of bond that is present in proteins. Proteins are macromolecules composed of amino acids that are linked together by peptide bonds to form long chains called polypeptides. These polypeptide chains then fold and interact with each other to form the functional three-dimensional structure of proteins.

Peptide bonds are formed through a condensation reaction between the carboxyl group of one amino acid and the amino group of another amino acid. During this reaction, a water molecule is eliminated, and a covalent bond is formed between the carbon atom of the carboxyl group and the nitrogen atom of the amino group. This bond is known as a peptide bond.

Peptide bonds are stable and resistant to hydrolysis under normal physiological conditions. They have a partial double bond character due to resonance between the carbon and nitrogen atoms, which restricts rotation around the bond. This rigidity contributes to the overall stability and structural integrity of proteins.

Proteins are built from a linear sequence of amino acids, and the specific arrangement of amino acids determines the unique structure and function of each protein. The sequence of amino acids in a protein is determined by the genetic code, which is encoded in DNA and transcribed into messenger RNA. The ribosome, a cellular machinery, then translates the mRNA sequence into a polypeptide chain by joining the amino acids together through peptide bonds.

In summary, peptide bonds are the specific type of bond present in proteins. These bonds are formed between amino acids and play a crucial role in determining the structure, stability, and function of proteins.