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Proteins

95 questions found

Practice Questions

Phospholipids contribute directly to membrane function by

A. Storing genetic information
B. Forming a selectively permeable barrier
C. Producing ATP
D. Catalyzing protein synthesis

Their bilayer regulates movement of substances across membranes.

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Jun 29, 2026

During complete hydrolysis, phospholipids yield

A. Glycerol, fatty acids, phosphate and a nitrogen-containing group
B. Only glycerol
C. Only phosphate
D. Three amino acids

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

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Jun 29, 2026

The energy density of lipids exceeds carbohydrates because lipids are

A. More oxidized
B. More reduced
C. Rich in phosphate
D. Rich in nitrogen

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

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Jun 29, 2026

Biological membranes maintain structural integrity mainly because phospholipids arrange into

A. Monolayers
B. Bilayers
C. Micelles only
D. Protein sheets

The phospholipid bilayer provides stability while remaining fluid.

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Jun 29, 2026

Acylglycerols containing one fatty acid attached to glycerol are known as

A. Monoglycerides
B. Diglycerides
C. Triglycerides
D. Phosphoglycerides

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

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Jun 29, 2026

Digestion of dietary fats is facilitated by bile salts because they

A. Hydrolyze triglycerides
B. Emulsify fats
C. Produce glycerol
D. Synthesize phospholipids

Bile salts break large fat droplets into smaller droplets, increasing surface area for lipase.

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Jun 29, 2026

The fundamental structural feature common to all standard amino acids found in proteins is the presence of

A. An amino group and a carboxyl group attached to the same α-carbon atom
B. A sulfhydryl group and a hydroxyl group on the β-carbon
C. A purine ring and a phosphate group
D. An aromatic ring and a guanidinium group

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.

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Jun 29, 2026

Fatty acids containing only single covalent bonds between carbon atoms are

A. Unsaturated
B. Saturated
C. Aromatic
D. Branched-chain alcohols

Saturated fatty acids lack carbon-carbon double bonds.

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Jun 29, 2026

In living organisms, the classification of an amino acid as essential implies that it

A. Is the most abundant amino acid in protein structures
B. Can be synthesized by the body from metabolic intermediates
C. Cannot be synthesized de novo by the organism and must be obtained from the diet
D. Functions exclusively as an enzyme cofactor

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.

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Jun 29, 2026

The tertiary structure of a water-soluble globular protein is mainly driven by

A. Formation of glycosidic bonds
B. Burial of hydrophobic side chains inside the protein
C. Complete ionization of all amino acids
D. Peptide bond formation

The hydrophobic effect causes non-polar side chains to cluster in the interior, minimizing contact with water and stabilizing the folded structure.

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Jun 29, 2026

The quaternary structure of a protein refers to

A. Amino acid sequence
B. Folding of one polypeptide chain
C. Association of multiple folded polypeptide subunits
D. Formation of peptide bonds

Quaternary structure exists only in proteins composed of more than one polypeptide chain, such as hemoglobin.

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Jun 29, 2026

The most abundant amino acid in collagen is

A. Cysteine
B. Glycine
C. Lysine
D. Tryptophan

Collagen contains the repeating sequence Gly-X-Y. Glycine occurs every third residue, allowing tight packing of the triple helix.

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Jun 29, 2026

Protein denaturation by heat generally does not break

A. Hydrogen bonds
B. Ionic bonds
C. Hydrophobic interactions
D. Covalent peptide bonds

Heat disrupts weak interactions but usually leaves the covalent peptide backbone intact.

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Jun 29, 2026

Molecular chaperones such as Hsp70 primarily function by

A. Synthesizing peptide bonds
B. Preventing aggregation of unfolded proteins and assisting correct folding
C. Breaking disulfide bonds
D. Degrading proteins

Chaperones bind exposed hydrophobic regions of unfolded proteins, preventing aggregation and promoting correct folding.

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Jun 29, 2026

Histidine is commonly found in enzyme active sites because its imidazole side chain can

A. Form peptide bonds
B. Donate and accept protons near physiological pH
C. Form disulfide bonds
D. Bind DNA specifically

Histidine's pKa is close to physiological pH, making it ideal for acid-base catalysis.

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Jun 29, 2026

Adjacent strands in β-sheets may run in the same or opposite directions. These arrangements are called

A. Cis and trans
B. Parallel and antiparallel
C. Right-handed and left-handed
D. Axial and equatorial

β-sheets are classified according to the orientation of adjacent strands.

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Jun 29, 2026

The prosthetic group present in hemoglobin contains

A. Zinc
B. Iron
C. Magnesium
D. Copper

The heme prosthetic group contains Fe²⁺, which reversibly binds oxygen.

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Jun 29, 2026

A functional protein differs from a simple polypeptide because it

A. Is always multimeric
B. Has a stable three-dimensional conformation required for activity
C. Contains only essential amino acids
D. Always contains a prosthetic group

Protein function depends on proper folding into the native three-dimensional structure.

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Jun 29, 2026

Disulfide bonds are most commonly formed in the

A. Cytosol
B. Endoplasmic reticulum
C. Nucleus
D. Mitochondrial matrix

The oxidizing environment of the endoplasmic reticulum promotes the formation of disulfide bonds in secreted and membrane proteins.

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Jun 29, 2026
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