Step 1: Tertiary structure of proteins.
The tertiary structure of proteins refers to the overall 3D shape of the polypeptide chain, which is stabilized by various interactions such as hydrogen bonding, disulfide bonds, hydrophobic interactions, and van der Waals forces. The tertiary structure plays a crucial role in the function of the protein.
Step 2: Analyzing the statements.
- Statement (A) is incorrect because changes in pH can disrupt the tertiary structure of proteins. A change in pH can affect the ionization of amino acid side chains, which can alter the protein's structure and function. For example, pH changes can break ionic bonds and hydrogen bonds, causing the protein to denature.
- Statement (B) is correct. The tertiary structure is stabilized by a variety of forces, including hydrogen bonds, disulfide bonds (covalent bonds between cysteine residues), van der Waals interactions, and electrostatic (Coulombic) forces between charged side chains.
- Statement (C) is correct. The tertiary structure can be globular or fibrous depending on the type of protein. Globular proteins are generally compact and spherical, while fibrous proteins are elongated and form structural components of cells and tissues.
- Statement (D) is correct. The folding of the polypeptide chain into its functional 3D structure involves the positioning and orientation of the amino acids. The sequence of amino acids determines the folding pattern, which is critical for the protein's tertiary structure.
Step 3: Conclusion.
Since statement (A) is incorrect, the correct answer is (A).
Final Answer: (A) With change in pH tertiary structure of protein does not get disrupted.