DAT Biology Mock Exam
2026
Master Exam Prep Bundle
(Verified Questions & Answers)
A+ Grade Guaranteed
,atom made up of neutrons, protons, and electrons
molecules groups of 2 or more atoms joined via chemical bonds. chemical bonds are due to
electron interactions.
electronegativity defines the ability of an atom to attract electrons.
intramolecular bonds ionic and covalent bonds
intermolecular bonds hydrogen bonds
ionic bond complete transfer of electrons from one atom to another.
electronegativity of atoms are very different.
ex) NaCl
covalent bond electrons are shared between atoms.
nonpolar covalent bond equal sharing of electrons between atoms.
electronegativity of atoms are equal.
ex) Cl2
polar covalent bond unequal sharing of electrons between atoms.
forms a dipole.
electronegativity of atoms are slightly different.
ex) HCl
dipole electrons spend more time around one atom, giving that atom slight negative
charge and the other a slight positive charge.
hydrogen bond a weak intermolecular bond between molecules that results when a hydrogen
attached to a highly electronegative atom is attracted to the negative charge on
another molecule (with an F, O, or N atom).
ex) between H2O molecules
monomers single units polymers
polymers series of repeating monomers
functional groups specific cluster of atoms that give molecules unique properties. these are often
referred to as R groups.
sulfhydryl
2026
,monosaccharides single sugar molecules.
ex) glucose, fructose, galactose
alpha vs beta carbon is based on the position of H and OH on the 1st (anomeric)
carbon (OH down = alpha, OH up = beta)
disaccharides two sugar molecules joined together by a glycosidic linkage.
e.g. sucrose (glucose + fructose), lactose (glucose + galactose), maltose (glucose +
glucose)
glycosidic linkage joined by dehydration
polysaccharides a series of connected monosaccharides (an example of a polymer).
bonded together via dehydration synthesis and broken via hydrolysis.
alpha-glucose polymer carbohydrates starch
glycogen
starch functions to store energy in plant cells. consists primarily of amylose and
amylopectin.
glycogen functions to store energy in animal cells. differs from starch in its polymer branching.
beta glucose polymer carbohydrates cellulose
chitin
cellulose functions as a structural molecule for the walls of plant cells and wood.
chitin functions as a structural molecule in fungal cell walls & arthropod exoskeletons.
structurally similar to cellulose but with nitrogen-containing groups attached to each
B-glucose ring.
Polymers of amino acids joined by peptide bonds
Amino acid structure Central α-carbon bonded to H, NH2, COOH and a variable R
group
Fibrous protein Insoluble, long polymer ibers/sheets, form structural components of cells.
ex) collagen
Globular protein Soluble, folded tightly, perform many functions.
ex) albumin
Intermediate protein Soluble, fiber shaped, perform many functions.
ex) fibrinogen
2026
, simple protein Only amino acids.
ex) albumin
Conjugated protein Amino acids + non‐protein components.
ex) glycoprotein (mucin), metalloprotein (hemoglobin), lipoprotein (HDL/LDL)
primary structure of a protein amino acid sequence
secondary structure of a protein the 3D shape that results from its hydrogen
bonding between amino and carboxyl groups of adjacent amino acids. Secondary
structures
include the alpha helix and beta sheet.
tertiary structure of a protein 3D structure due to noncovalent interactions
between the R-groups of amino acids. These interactions include hydrogen
bonding, ionic bonding, hydrophobic effect (R-groups are pushed away from the
water center), disulfide bonds (the covalent exception to tertiary structure), and Van
der Waals forces.
quaternary structure of a protein the 3D structure from the grouping of two or more separate peptide chains.
protein denaturation any secondary, tertiary, and quaternary structure is removed but the amino acid
sequence (primary structure) remains intact. Protein denaturation usually occurs
from excess temperature, chemical stress, pH variance, heavy metal salts, and
radiation. A protein's 3D structure is critical to its function -loss of shape due to
denaturation leads to loss of function.
storage proteins biological reserves of amino acids.
ex) ovalbumin (egg whites), casein (milk), plant seeds
transport proteins movement of substances within and between cells.
ex) hemoglobin (transport oxygen), cytochromes (carry electrons)
Hormone proteins signaling molecules circulated throughout the body to regulate organs.
ex) growth hormone, prolactin, glucagon Covered in more detail in the endocrine
section
Receptor proteins membrane proteins that bind ions and signaling molecules, causing changes on a
cellular level.
ex) insulin receptors, ligand‐gated ion channels
motion proteins movement generated at a cellular or at the level of the entire organism.
ex) tubulin (flagella ‐cell movement), actin and myosin (skeletal muscles - organism
movement)
structure proteins strengthen and support tissues.
ex) collagen (connective tissue), keratin (nails)
immune defense proteins prevent and protect against pathogen attack.
ex) antibodies
2026
2026
Master Exam Prep Bundle
(Verified Questions & Answers)
A+ Grade Guaranteed
,atom made up of neutrons, protons, and electrons
molecules groups of 2 or more atoms joined via chemical bonds. chemical bonds are due to
electron interactions.
electronegativity defines the ability of an atom to attract electrons.
intramolecular bonds ionic and covalent bonds
intermolecular bonds hydrogen bonds
ionic bond complete transfer of electrons from one atom to another.
electronegativity of atoms are very different.
ex) NaCl
covalent bond electrons are shared between atoms.
nonpolar covalent bond equal sharing of electrons between atoms.
electronegativity of atoms are equal.
ex) Cl2
polar covalent bond unequal sharing of electrons between atoms.
forms a dipole.
electronegativity of atoms are slightly different.
ex) HCl
dipole electrons spend more time around one atom, giving that atom slight negative
charge and the other a slight positive charge.
hydrogen bond a weak intermolecular bond between molecules that results when a hydrogen
attached to a highly electronegative atom is attracted to the negative charge on
another molecule (with an F, O, or N atom).
ex) between H2O molecules
monomers single units polymers
polymers series of repeating monomers
functional groups specific cluster of atoms that give molecules unique properties. these are often
referred to as R groups.
sulfhydryl
2026
,monosaccharides single sugar molecules.
ex) glucose, fructose, galactose
alpha vs beta carbon is based on the position of H and OH on the 1st (anomeric)
carbon (OH down = alpha, OH up = beta)
disaccharides two sugar molecules joined together by a glycosidic linkage.
e.g. sucrose (glucose + fructose), lactose (glucose + galactose), maltose (glucose +
glucose)
glycosidic linkage joined by dehydration
polysaccharides a series of connected monosaccharides (an example of a polymer).
bonded together via dehydration synthesis and broken via hydrolysis.
alpha-glucose polymer carbohydrates starch
glycogen
starch functions to store energy in plant cells. consists primarily of amylose and
amylopectin.
glycogen functions to store energy in animal cells. differs from starch in its polymer branching.
beta glucose polymer carbohydrates cellulose
chitin
cellulose functions as a structural molecule for the walls of plant cells and wood.
chitin functions as a structural molecule in fungal cell walls & arthropod exoskeletons.
structurally similar to cellulose but with nitrogen-containing groups attached to each
B-glucose ring.
Polymers of amino acids joined by peptide bonds
Amino acid structure Central α-carbon bonded to H, NH2, COOH and a variable R
group
Fibrous protein Insoluble, long polymer ibers/sheets, form structural components of cells.
ex) collagen
Globular protein Soluble, folded tightly, perform many functions.
ex) albumin
Intermediate protein Soluble, fiber shaped, perform many functions.
ex) fibrinogen
2026
, simple protein Only amino acids.
ex) albumin
Conjugated protein Amino acids + non‐protein components.
ex) glycoprotein (mucin), metalloprotein (hemoglobin), lipoprotein (HDL/LDL)
primary structure of a protein amino acid sequence
secondary structure of a protein the 3D shape that results from its hydrogen
bonding between amino and carboxyl groups of adjacent amino acids. Secondary
structures
include the alpha helix and beta sheet.
tertiary structure of a protein 3D structure due to noncovalent interactions
between the R-groups of amino acids. These interactions include hydrogen
bonding, ionic bonding, hydrophobic effect (R-groups are pushed away from the
water center), disulfide bonds (the covalent exception to tertiary structure), and Van
der Waals forces.
quaternary structure of a protein the 3D structure from the grouping of two or more separate peptide chains.
protein denaturation any secondary, tertiary, and quaternary structure is removed but the amino acid
sequence (primary structure) remains intact. Protein denaturation usually occurs
from excess temperature, chemical stress, pH variance, heavy metal salts, and
radiation. A protein's 3D structure is critical to its function -loss of shape due to
denaturation leads to loss of function.
storage proteins biological reserves of amino acids.
ex) ovalbumin (egg whites), casein (milk), plant seeds
transport proteins movement of substances within and between cells.
ex) hemoglobin (transport oxygen), cytochromes (carry electrons)
Hormone proteins signaling molecules circulated throughout the body to regulate organs.
ex) growth hormone, prolactin, glucagon Covered in more detail in the endocrine
section
Receptor proteins membrane proteins that bind ions and signaling molecules, causing changes on a
cellular level.
ex) insulin receptors, ligand‐gated ion channels
motion proteins movement generated at a cellular or at the level of the entire organism.
ex) tubulin (flagella ‐cell movement), actin and myosin (skeletal muscles - organism
movement)
structure proteins strengthen and support tissues.
ex) collagen (connective tissue), keratin (nails)
immune defense proteins prevent and protect against pathogen attack.
ex) antibodies
2026
