BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Cysteine, by virtue of its ability to form disulfide bonds, plays a crucial role in protein structure and in protein-folding pathways. Methionine metabolism begins with its activation to S-adenosylmethionine.

Detailed explanation-2: -Cysteine, which is abbreviated with the letters Cys or just C, is one of the 20 amino acids that make up proteins in our body. Cysteine’s R group is made up of a 1-carbon structure with a sulfhydryl group attached to the end. This makes it a polar, hydrophilic, and uncharged amino acid.

Detailed explanation-3: -Methionine and cysteine are the two primary sulfur-containing amino acids in mammals. Methionine is an essential amino acid, obtained by dietary intake while cysteine is non-essential and a metabolite of methionine metabolism.

Detailed explanation-4: -The –SH or sulfhydryl groups are present in the R group of cysteine amino acids. When two cysteine molecules are in close proximity, the sulfhydryl group present between them oxidizes and forms a bond called a disulfide bond a functional group.

Detailed explanation-5: -The other sulfur-containing amino acid, methionine, cannot form disulfide bonds.