Final answer:
The true statement about disulfide bonds is that they stabilize a protein's final conformation without changing it. These bonds form by the oxidation of the sulfhydryl groups of cysteine residues and are typically found in proteins that are not in the cytosol. Agents like b-mercaptoethanol break these bonds through reduction.
Step-by-step explanation:
The statement that is true regarding disulfide bonds is that they stabilize but do not change a protein's final conformation. Disulfide bonds are covalent bonds formed through the oxidation of two cysteine amino acids within a protein. This oxidation reaction results from the sulfur atoms in the sulfhydryl (-SH) groups of cysteine residues forming a strong covalent bond known as a disulfide linkage (-S-S
Disulfide bonds are more commonly found in proteins that are secreted or in extracellular environments because the cytosol is a reducing environment where disulfide bonds are less stable. Agents such as b-mercaptoethanol can break disulfide bonds through reduction, not oxidation, contradicting the typo 'mayor at T ethanol' and its mentioned mechanism.
The formation of a disulfide bond is indeed a stabilizing factor for a protein's tertiary structure and is crucial in determining the three-dimensional folding pattern that is necessary for the protein's functional configuration.