To solve the problem, we need to explain the difference between native and denatured proteins.
1. Understanding Proteins:
Proteins are large, complex molecules made up of amino acid chains, which fold into specific three-dimensional structures that determine their function. The structure of a protein plays a critical role in its biological activity, and changes to this structure can significantly affect its function.
2. Native Protein:
Native proteins are proteins that have their natural, functional three-dimensional structure. In this state, the protein's secondary, tertiary, and sometimes quaternary structures are intact, allowing the protein to perform its specific biological function. These structures are stabilized by various forces, including hydrogen bonds, ionic interactions, hydrophobic interactions, and disulfide bridges.
3. Denatured Protein:
Denatured proteins are proteins whose three-dimensional structure has been altered, usually due to external factors such as heat, extreme pH, or the presence of certain chemicals. Denaturation disrupts the non-covalent bonds and sometimes even covalent bonds (like disulfide bridges) that maintain the protein's structure. This results in the unfolding or misfolding of the protein, which leads to the loss of its biological activity.
4. Key Differences:
- Structure: Native proteins have a well-defined, functional three-dimensional structure, while denatured proteins have an altered or unfolded structure.
- Function: Native proteins are functional, as their structure allows them to perform specific biological roles, while denatured proteins are typically non-functional due to their altered shape.
- Stability: Native proteins are stable under normal physiological conditions, while denatured proteins are often unstable and can lose their ability to bind to substrates or catalyze reactions.
5. Final Answer:
The main difference between native and denatured proteins is that native proteins retain their natural three-dimensional structure, allowing them to function properly, while denatured proteins have lost their native structure and thus their biological activity, typically due to environmental stress factors like heat or pH changes.
Write IUPAC names of the following compounds and classify them into primary, secondary and tertiary amines.
(i) (CH3 )2CHNH2 (ii) CH3 (CH2 )2NH2 (iii) CH3NHCH(CH3 )2
(iv) (CH3 )3CNH2 (v) C6H5NHCH3 (vi) (CH3CH2 )2NCH3 (vii) m–BrC6H4NH2
Give one chemical test to distinguish between the following pairs of compounds.
(i) Methylamine and dimethylamine
(ii) Secondary and tertiary amines
(iii) Ethylamine and aniline
(iv) Aniline and benzylamine
(v) Aniline and N-methylaniline
Account for the following:
(i) pKb of aniline is more than that of methylamine.
(ii) Ethylamine is soluble in water whereas aniline is not.
(iii) Methylamine in water reacts with ferric chloride to precipitate hydrated ferric oxide.
(iv) Although amino group is o– and p– directing in aromatic electrophilic substitution reactions, aniline on nitration gives a substantial amount of m-nitroaniline.
(v) Aniline does not undergo Friedel-Crafts reaction.
(vi) Diazonium salts of aromatic amines are more stable than those of aliphatic amines. (vii) Gabriel phthalimide synthesis is preferred for synthesising primary amines.