Key Words
ENGINEERING PROTEINS
Acid derivatives
Active site
Amino acid
Base pairs
Bifunctional Compounds
Chiral
Closed system
Codons &
Anti-codons
D or L-optical isomers
Denatured
DNA
Dynamic equilibrium
Equilibrium constant
First order reaction
(enzymes)
Gene
Genome
Half-life
Helix/sheet
Compounds with functional groups based on carboxylic acid
(-COOH ) see table p300 in Chemical Ideas e.g.
Ester –COOR, Acyl chloride –COCl, Amide -CONH2
Acid anhydride -(CO)2O
The region in an enzyme into which the substrate binds
before it reacts with it.
An organic molecule that contains both an –NH2 group and
a –COOH group
Pairs of bases that fit neatly together thus placing groups
in just the right positions for hydrogen bonds to form.
These can be seen in the DNA double helix.
Compounds which have two functional groups e.g. amino
acids have -NH2 and -COOH.
A carbon centre within a molecule surrounded by four
different groupings of atoms (=> non-superimposable
mirror images).
One where no chemicals can enter or leave e.g. a
stoppered flask.
Codons are the different combinations of triplet codes that
define a particular amino acid. Anti-codons allow tRNA
molecules to recognise and bind onto the codons on mRNA,
e.g. G & C recognise one another and so do U & A.
The two mirror image forms of an enantiomer – one
rotates plane polarised light to the right (dextro-rotatory)
while the other rotates it to the left (laevo-rotatory).
A term used to describe the destruction of the active sites
in a protein caused by the loss of shape when the tertiary
structure is broken.
Deoxyribonucleic acid
A reversible reaction in which forward and reverse
reactions proceed simultaneously but there is no overall
change in any of the concentrations.
A constant calculated for a reversible reaction, as follows:
For the reaction aA + bB  cC + dD
The equilibrium constant is: Kc = Cc Dd / Aa Bb
One in which the reaction rate is directly proportional to
the substrate concentration.
A DNA segment responsible for a particular protein (DNA
codes for RNA which, in turn codes for proteins)
The full set of all the genes of an organism.
The time taken for half of a particular reagent in a reaction
to become used up.
Hydrogen bonding causes regular folding or twisting of
protein chains. The helix is a tight coil of protein chain
while extended chains can be bonded into a sheet.
Hydrogen bonding
Initial rate
Instantaneous dipole induced dipole
Insulin
Intermediates
Macroscopic scale
Mechanism
Microscopic scale
mRNA
NMR
Optical isomers
(enantiomers)
Order of reaction
Overall order
Polypeptide
Position of equilibrium
Primary structure (of a
protein)
Quaternary structure
Rate determining step
Rate equation
Ribosome
RNA
Secondary structure
Steady state
Substrate
Tertiary structure
A particularly strong type of intermolecular force of
attraction in which highly polar N-H, O-H, or F-H bonds in
molecules cause very strong dipole-dipole attraction
between molecules.
The rate of a chemical reaction at the start.
A type of intermolecular attraction in which temporary
dipoles in one molecule induces a dipole in a neighbouring
molecule and then attracts it.
A hormone produced in the pancreas that controls the
uptake of glucose and some other sugars by our cells.
Chemicals formed in the middle of a reaction mechanism
The scale that we as humans are used to – test tubes and
flasks!
The series of separate steps that make up a reaction.
Individual molecule scale
Messenger ribonucleic acid. It carries the code for protein
synthesis.
Nuclear magnetic resonance – a type of spectroscopy in
which the number and type of grouping that hydrogen
nuclei exist in within a molecule can be determined.
Mirror image molecules (ones that are nonsuperimposable).
The power to which the concentration of a reactant in a
rate equation must be raised.
The sum of the separate orders in a rate equation.
A polymer containing up to 40 amino acid residues joined
by peptide links.
The term that describes the relative concentrations of
products to reactants in an equilibrium
The order of amino acids in the protein.
The joining of insulin monomers into a hexamer
The slowest step of the separate steps that make up a
mechanism.
An equation which links the rate of a reaction to the initial
concentrations of the reactants:
e.g. for the reaction: A + B  products
the rate equation is: rate = k Am Bn
where m is the order of reaction with respect to A and n is
the order of reaction with respect to B.
A cell’s catalyst for protein production.
Ribonucleic acid
The coiling of parts of the protein chain into a helix or the
formation of a region of sheet
This can occur in an open system where the concentrations
of products and reactants in a series of reactions remains
constant i.e. there is no overall change.
A molecule that reacts with a particular enzyme.
The overall shape of a protein – the folding of the
secondary structure into an insulin monomer.
Triplet code
tRNA
Zero order reaction
(enzymes)
Zwitterion
A code consisting of a combination of three bases (from
U,C,A,G) that tells a cell which amino acids to use to build
a protein
Transfer ribonucleic acid – collects an amino acid and takes
it into the mRNA strand.
One in which the reaction rate does not depend on the
substrate concentration.
An ion containing both positively and negatively charged
groups.