DAT Bootcamp Chapter 1 Study Guide –
Molecules & Fundamentals of Biology
(Biochemistry, Macromolecules & Cell
Basics Review 2026)
intramolecular
ionic and covalent bonds are (intermolecular/intramolecular)
intermolecular
hydrogen bonds are (intermolecular/intramolecular)
down
a sugar molecule is classified as alpha if the OH group points _____ on the first carbon
up
a sugar molecule is classified as beta if the OH group points _____ on the first carbon
starch, glycogen
name two alpha-glucose polymer carbohydrates
cellulose, chitin
name two beta-glucose polymer carbohydrates
starch
carb that functions to store energy in plant cells; consists primarily of amylose and
amylopectin
glycogen
carb that functions to store energy in animal cells; differs from starch in its polymer
branching
cellulose
carb that functions as a structural molecule for the walls of plant cells and wood
chitin
carb that functions as a structural molecule in fungal cell walls & arthropod
exoskeletons; structurally similar to cellulose but with nitrogen-containing groups
attached to each β-glucose ring
proteins
polymers of amino acids joined by peptide bonds
H, NH₂, COOH, R
in an amino acid, what 4 things is the central carbon bonded to?
dehydration
in a protein, amino acids form peptide bonds with one another via _____ synthesis
peptide bonds
what type of bonds link amino acids in proteins?
fibrous
structural classification of protein: insoluble, long polymer fibers/sheets, form structural
components of cells; example: collagen
globular
, structural classification of protein: soluble, folded tightly, perform many functions;
example: albumin
intermediate
structural classification of protein: soluble, fiber shaped, perform many functions;
example: fibrinogen
simple
composition classification of protein: only amino acids; example: albumin
conjugated
composition classification of protein: amino acids + non-protein components; examples:
glycoprotein, metalloprotein, lipoprotein
primary
the _____ structure of a protein is its amino acid sequence
secondary
the _____ structure of a protein is the 3D shape that results from its hydrogen bonding
between amino and carboxyl groups of adjacent amino acids; includes alpha helix and
beta sheet
tertiary
the _____ structure of a protein is the 3D structure due to non-covalent interactions
between the R-groups of amino acids; these interactions include hydrogen bonding,
ionic bonding, hydrophobic effect, disulfide bonds, and Van der Waals forces
quaternary
the _____ structure of a protein is the 3D structure from the grouping of two or more
separate peptide chains
protein denaturation
during _____ any secondary, tertiary, and quaternary structure is removed, but the
amino acid sequence remains intact; usually occurs from excess temperature, chemical
stress, pH variance, heave metal salts, and radiation
ribozymes
not all enzymes are proteins; some are RNA molecules called _____
temperature, pH
enzyme efficiency is determined by _____ and _____
induced fit
enzymes bind at the active site via _____
cofactors
non-protein molecules that assist enzymes (usually by donating or accepting some
component of a reaction like electrons)
coenzymes
organic cofactors (e.g. vitamins)
metal ions
inorganic cofactors are usually _____
prosthetic group
A cofactor that binds tightly/covalently to an enzyme is referred to as a _____
apoenzyme
an enzyme without its cofactor
holoenzyme
Molecules & Fundamentals of Biology
(Biochemistry, Macromolecules & Cell
Basics Review 2026)
intramolecular
ionic and covalent bonds are (intermolecular/intramolecular)
intermolecular
hydrogen bonds are (intermolecular/intramolecular)
down
a sugar molecule is classified as alpha if the OH group points _____ on the first carbon
up
a sugar molecule is classified as beta if the OH group points _____ on the first carbon
starch, glycogen
name two alpha-glucose polymer carbohydrates
cellulose, chitin
name two beta-glucose polymer carbohydrates
starch
carb that functions to store energy in plant cells; consists primarily of amylose and
amylopectin
glycogen
carb that functions to store energy in animal cells; differs from starch in its polymer
branching
cellulose
carb that functions as a structural molecule for the walls of plant cells and wood
chitin
carb that functions as a structural molecule in fungal cell walls & arthropod
exoskeletons; structurally similar to cellulose but with nitrogen-containing groups
attached to each β-glucose ring
proteins
polymers of amino acids joined by peptide bonds
H, NH₂, COOH, R
in an amino acid, what 4 things is the central carbon bonded to?
dehydration
in a protein, amino acids form peptide bonds with one another via _____ synthesis
peptide bonds
what type of bonds link amino acids in proteins?
fibrous
structural classification of protein: insoluble, long polymer fibers/sheets, form structural
components of cells; example: collagen
globular
, structural classification of protein: soluble, folded tightly, perform many functions;
example: albumin
intermediate
structural classification of protein: soluble, fiber shaped, perform many functions;
example: fibrinogen
simple
composition classification of protein: only amino acids; example: albumin
conjugated
composition classification of protein: amino acids + non-protein components; examples:
glycoprotein, metalloprotein, lipoprotein
primary
the _____ structure of a protein is its amino acid sequence
secondary
the _____ structure of a protein is the 3D shape that results from its hydrogen bonding
between amino and carboxyl groups of adjacent amino acids; includes alpha helix and
beta sheet
tertiary
the _____ structure of a protein is the 3D structure due to non-covalent interactions
between the R-groups of amino acids; these interactions include hydrogen bonding,
ionic bonding, hydrophobic effect, disulfide bonds, and Van der Waals forces
quaternary
the _____ structure of a protein is the 3D structure from the grouping of two or more
separate peptide chains
protein denaturation
during _____ any secondary, tertiary, and quaternary structure is removed, but the
amino acid sequence remains intact; usually occurs from excess temperature, chemical
stress, pH variance, heave metal salts, and radiation
ribozymes
not all enzymes are proteins; some are RNA molecules called _____
temperature, pH
enzyme efficiency is determined by _____ and _____
induced fit
enzymes bind at the active site via _____
cofactors
non-protein molecules that assist enzymes (usually by donating or accepting some
component of a reaction like electrons)
coenzymes
organic cofactors (e.g. vitamins)
metal ions
inorganic cofactors are usually _____
prosthetic group
A cofactor that binds tightly/covalently to an enzyme is referred to as a _____
apoenzyme
an enzyme without its cofactor
holoenzyme
