DAT Biology Review Practice Exam
Questions & Answers.
atom - CORRECT ANSWER made up of neutrons, protons, and electrons
molecules - CORRECT ANSWER groups of 2 or more atoms joined via chemical bonds. chemical bonds
are due to electron interactions.
electronegativity - CORRECT ANSWER defines the ability of an atom to attract electrons.
intramolecular bonds - CORRECT ANSWER ionic and covalent bonds
intermolecular bonds - CORRECT ANSWER hydrogen bonds
ionic bond - CORRECT ANSWER complete transfer of electrons from one atom to another.
electronegativity of atoms are very different.
ex) NaCl
covalent bond - CORRECT ANSWER electrons are shared between atoms.
nonpolar covalent bond - CORRECT ANSWER equal sharing of electrons between atoms.
electronegativity of atoms are equal.
ex) Cl2
polar covalent bond - CORRECT ANSWER unequal sharing of electrons between atoms.
forms a dipole.
electronegativity of atoms are slightly different.
ex) HCl
,dipole - CORRECT ANSWER electrons spend more time around one atom, giving that atom slight
negative charge and the other a slight positive charge.
hydrogen bond - CORRECT ANSWER 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 - CORRECT ANSWER single units polymers
polymers - CORRECT ANSWER series of repeating monomers
functional groups - CORRECT ANSWER specific cluster of atoms that give molecules unique properties.
these are often referred to as R groups.
sulfhydryl - CORRECT ANSWER
monosaccharides - CORRECT ANSWER 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 - CORRECT ANSWER two sugar molecules joined together by a glycosidic linkage.
e.g. sucrose (glucose + fructose), lactose (glucose + galactose), maltose (glucose + glucose)
glycosidic linkage - CORRECT ANSWER joined by dehydration
polysaccharides - CORRECT ANSWER a series of connected monosaccharides (an example of a polymer).
bonded together via dehydration synthesis and broken via hydrolysis.
,alpha-glucose polymer carbohydrates - CORRECT ANSWER starch
glycogen
starch - CORRECT ANSWER functions to store energy in plant cells. consists primarily of amylose and
amylopectin.
glycogen - CORRECT ANSWER functions to store energy in animal cells. differs from starch in its polymer
branching.
beta glucose polymer carbohydrates - CORRECT ANSWER cellulose
chitin
cellulose - CORRECT ANSWER functions as a structural molecule for the walls of plant cells and wood.
chitin - CORRECT ANSWER 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 - CORRECT ANSWER peptide bonds
Amino acid structure - CORRECT ANSWER Central α-carbon bonded to H, NH2, COOH and a variable R
group
Fibrous protein - CORRECT ANSWER Insoluble, long polymer ibers/sheets, form structural components
of cells.
ex) collagen
Globular protein - CORRECT ANSWER Soluble, folded tightly, perform many functions.
ex) albumin
, Intermediate protein - CORRECT ANSWER Soluble, fiber shaped, perform many functions.
ex) fibrinogen
simple protein - CORRECT ANSWER Only amino acids.
ex) albumin
Conjugated protein - CORRECT ANSWER Amino acids + non ‐protein components.
ex) glycoprotein (mucin), metalloprotein (hemoglobin), lipoprotein (HDL/LDL)
primary structure of a protein - CORRECT ANSWER amino acid sequence
secondary structure of a protein - CORRECT ANSWER 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 - CORRECT ANSWER 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 - CORRECT ANSWER the 3D structure from the grouping of two or
more separate peptide chains.
protein denaturation - CORRECT ANSWER 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 - CORRECT ANSWER biological reserves of amino acids.
ex) ovalbumin (egg whites), casein (milk), plant seeds
Questions & Answers.
atom - CORRECT ANSWER made up of neutrons, protons, and electrons
molecules - CORRECT ANSWER groups of 2 or more atoms joined via chemical bonds. chemical bonds
are due to electron interactions.
electronegativity - CORRECT ANSWER defines the ability of an atom to attract electrons.
intramolecular bonds - CORRECT ANSWER ionic and covalent bonds
intermolecular bonds - CORRECT ANSWER hydrogen bonds
ionic bond - CORRECT ANSWER complete transfer of electrons from one atom to another.
electronegativity of atoms are very different.
ex) NaCl
covalent bond - CORRECT ANSWER electrons are shared between atoms.
nonpolar covalent bond - CORRECT ANSWER equal sharing of electrons between atoms.
electronegativity of atoms are equal.
ex) Cl2
polar covalent bond - CORRECT ANSWER unequal sharing of electrons between atoms.
forms a dipole.
electronegativity of atoms are slightly different.
ex) HCl
,dipole - CORRECT ANSWER electrons spend more time around one atom, giving that atom slight
negative charge and the other a slight positive charge.
hydrogen bond - CORRECT ANSWER 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 - CORRECT ANSWER single units polymers
polymers - CORRECT ANSWER series of repeating monomers
functional groups - CORRECT ANSWER specific cluster of atoms that give molecules unique properties.
these are often referred to as R groups.
sulfhydryl - CORRECT ANSWER
monosaccharides - CORRECT ANSWER 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 - CORRECT ANSWER two sugar molecules joined together by a glycosidic linkage.
e.g. sucrose (glucose + fructose), lactose (glucose + galactose), maltose (glucose + glucose)
glycosidic linkage - CORRECT ANSWER joined by dehydration
polysaccharides - CORRECT ANSWER a series of connected monosaccharides (an example of a polymer).
bonded together via dehydration synthesis and broken via hydrolysis.
,alpha-glucose polymer carbohydrates - CORRECT ANSWER starch
glycogen
starch - CORRECT ANSWER functions to store energy in plant cells. consists primarily of amylose and
amylopectin.
glycogen - CORRECT ANSWER functions to store energy in animal cells. differs from starch in its polymer
branching.
beta glucose polymer carbohydrates - CORRECT ANSWER cellulose
chitin
cellulose - CORRECT ANSWER functions as a structural molecule for the walls of plant cells and wood.
chitin - CORRECT ANSWER 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 - CORRECT ANSWER peptide bonds
Amino acid structure - CORRECT ANSWER Central α-carbon bonded to H, NH2, COOH and a variable R
group
Fibrous protein - CORRECT ANSWER Insoluble, long polymer ibers/sheets, form structural components
of cells.
ex) collagen
Globular protein - CORRECT ANSWER Soluble, folded tightly, perform many functions.
ex) albumin
, Intermediate protein - CORRECT ANSWER Soluble, fiber shaped, perform many functions.
ex) fibrinogen
simple protein - CORRECT ANSWER Only amino acids.
ex) albumin
Conjugated protein - CORRECT ANSWER Amino acids + non ‐protein components.
ex) glycoprotein (mucin), metalloprotein (hemoglobin), lipoprotein (HDL/LDL)
primary structure of a protein - CORRECT ANSWER amino acid sequence
secondary structure of a protein - CORRECT ANSWER 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 - CORRECT ANSWER 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 - CORRECT ANSWER the 3D structure from the grouping of two or
more separate peptide chains.
protein denaturation - CORRECT ANSWER 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 - CORRECT ANSWER biological reserves of amino acids.
ex) ovalbumin (egg whites), casein (milk), plant seeds
