Essential and Nonessential Amino Acids,
Conditionally Essential Amino Acids, Peptide
Bonds, Dipeptides, Tripeptides, Polypeptides,
Hemoglobin Structure and Function, Denaturation,
Enzymes and Proteases, Peptidases, Gene
Expression, Collagen and Connective Tissue
Proteins, Protein Turnover, Amino Acid Pool, High-
Quality Proteins, Limiting Amino Acids,
Complementary Proteins, Protein Digestibility,
Reference Proteins, Neurotransmitters, Fluid
Balance, Edema, Nitrogen Balance, Deamination,
Antigens and Antibodies, Immunity, Protein-Energy
Malnutrition, Acute and Chronic PEM, Marasmus,
Kwashiorkor, Dysentery, Whey Protein, and
Branched-Chain Amino Acids in Human Health and
Nutrition Exam Questions Verified and Provided
with A+ Graded Rationales Latest Updated 2026
proteins
compounds composed of carbon hydrogen, oxygen, and nitrogen atoms arranged into amino
acids linked in a chain. Some amino acids contain sulfur atoms
amino acids
building block of proteins. each contains an amino group, an acid group, a hydrogen atom, and a
distinctive side group, all attached to a central carbon atom
nonessential amino acids
amino acids that the body can synthesize
essential amino acids
amino acids that the body cannot synthesize in amounts sufficient to me physiological needs
, conditionally essential amino acids
an amino acid that is normally nonessential but must be supplied by the diet in special
circumstances when the need for it exceeds the body's ability to produce it
peptide bond
a bond that connects the acid end of one amino acid with the amino end of another, forming a
link in a protein chain
dipeptide
two amino acids bonded together
tripeptide
three amino acids bonded together
polypeptide
many (ten or more) amino acids bonded together
hemoglobin
the globular protein of the red blood cells that carries oxygen from the lungs to the cell
throughout the body.
denaturation
the change in a proteins shape and consequent loss of its function brought about by heat,
agitation, acid, base, alcohol, heavy metals, or other agents
pepsin
a gastric enzyme that hydrolyzes protein. blank is secreted in an inactive form, pepsinogen,
which is activated by hydrochloric acid in the stomach
proteases
enzyme that hydrolyze protein
peptidase
a digestive enzyme that hydrolyzes peptide bonds. tripeptidases cleave tripeptides; dipeptase
cleave dipeptides. Endopetidases cleave peptide bonds within chain to create smaller
fragments, whereas exopeptidases cleave bonds at the ends to release free amino acids.
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