MCQs

Complete acid hydrolysis (e.g., 6M HCl at 110°C for 24 hours) cleaves all peptide bonds in a protein, releasing the constituent free amino acids. Partial hydrolysis yields smaller peptides (di-, tri-, and oligopeptides).

In proline, the R-group forms a pyrrolidine ring by bonding back to the amide nitrogen. This cyclization eliminates the amide hydrogen needed for H-bonding in an α-helix and imposes a rigid, fixed kink in the polypeptide backbone, disrupting the regular helical conformation.

The thiol (-SH) group of cysteine's side chain can be oxidized to form a covalent disulfide bond (-S-S-) with another cysteine residue. This bond is critical for stabilizing the tertiary structure of secreted proteins like insulin and immunoglobulins. Methionine contains sulfur but cannot form disulfide bridges.

A carbon atom must be bonded to four different groups to be chiral. The α-carbon of glycine is bonded to an amino group, a carboxyl group, and two hydrogen atoms. Since two substituents are identical, it is not a chiral center, and glycine is optically inactive.

The pI is the pH where the net charge on the amino acid is zero. At this pH, the molecule is a zwitterion and will not move towards either the anode or cathode during electrophoresis. For neutral amino acids, pI is the average of pKₐ₁ and pKₐ₂.

At the isoelectric point (pI), the amino group is protonated (-NH₃⁺) and the carboxyl group is deprotonated (-COO⁻). The molecule carries equal positive and negative charges, making it electrically neutral overall, termed a zwitterion.

The α-carbon of 19 of the 20 standard amino acids is attached to four different groups, making it a chiral center. With very rare exceptions, ribosomes exclusively incorporate amino acids with the L-configuration into proteins. Glycine has two hydrogens and is thus achiral.

The peptide bond exhibits resonance between the carbonyl oxygen and the amide nitrogen. This resonance gives the C-N bond approximately 40% double-bond character, restricting rotation and making the six atoms of the peptide group lie in a single plane.

Essential amino acids lack the necessary biosynthetic pathways in the organism. For humans, there are nine essential amino acids (e.g., lysine, valine, phenylalanine). Non-essential amino acids can be synthesized from common metabolic intermediates.

All 20 standard amino acids (except proline, which is an imino acid) are α-amino acids. They contain a central α-carbon to which an amino group (-NH₂), a carboxyl group (-COOH), a hydrogen atom, and a variable R-group are attached.

A monoglyceride consists of glycerol esterified with a single fatty acid.

The phospholipid bilayer provides stability while remaining fluid.

Lipids contain more C-H bonds, producing more ATP during oxidation.

Phospholipids contain additional phosphate-containing head groups compared to triglycerides.

Their bilayer regulates movement of substances across membranes.

All three fatty acids attached to glycerol are the same in simple triglycerides.

Fatty acid chains repel water and face inward within the membrane.

Esterification releases one water molecule per ester bond formed.

Triglycerides lack phosphate groups and function mainly in energy storage.