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activation energy
amount of energy
required to get a
reaction started
active site
pocket or groove on the
surface of the enzyme
where catalysis occurs
allosteric site
place on an enzyme where a
molecule that is not a substrate
may bind, thus changing the
shape of the enzyme and
influencing its ability to be active.
amino acid
organic molecule with
amino and carboxyl
groups
catalyst
chemical agent that
changes the rate of a
reaction without being
consumed by the reaction
coenzyme
cofactor that is an
organic molecule
cofactor
nonprotein helpers for
catalytic activity
covalent bond
sharing of a pair of
valence electrons by
two atoms
dehydration reaction
denaturation
molecules connected by a
reaction where 2 molecules are
covalently bonded to each other
with loss of a water molecule
when proteins lose their
quaternary, tertiary, and
secondary structures as a
result of external stressors
enzyme
subgroup of catalysts
-proteins or protein-based
-highly specific
enzyme-substrate
complex
the intermediate formed
when a substrate molecule
interacts with the active
site of an enzyme
functional group
chemical groups affect
molecular function by
being directly involved in
chemical reactions
hydrogen bond
non-covalent attraction
between a hydrogen and
an electronegative atom
hydrophillic
any substance that has
an affinity for water
hydrophobic
substances that are nonionic and non-polar that
seem to repel water.
inhibitor
substance that slow down
or stops an enzyme
catalyzed reaction
isomer
compounds that have the same
numbers of atoms of the same
elements but different
structures and different
properties
monomer
repeating units that serve
as the building blocks of a
polymer
polar covalent bond
one atom is bonded to a
more electronegative
atom; electrons of bonds
are not shared equally.
polar molecule
overall charge of
molecule is unevenly
distributed
polymer
long molecule consisting
of many similar or
identical building blocks
linked by covalent bonds
polypeptide
polymer of many
amino acids linked by
peptide bonds
polypeptide bond
bonds that hold
together amino acids
in a polypeptide chain
primary structure
unique linear sequence
of amino acids
protein
consist of one or more
polypeptides folded and
coiled into specific
conformations
quaternary structure
proteins that consist of
more than one
polypeptide chain.
secondary structure
how the polypeptide
coils or folds into two
distinct shapes
substrate
reactants in enzyme
assisted reactions
tertiary structure
intricate three-dimensional
shape or conformation of a
protein that is superimposed
on its secondary structure
Van der Waals
interaction
ever-changing regions of
positive and negative charge
that enable all atoms and
molecules to stick to one
another