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UNIT ONE
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PEPTIDE BOND
THE BOND BETWEEN THE AMINE GROUP OF ONE AMINO ACID AND THE CARBOXYL GROUP OF ANOTHER.
POLYPEPTIDE
IN A POLYPEPTIDE THERE IS ALWAYS ONE END WITH A FREE AMINO (NH2) GROUP: N-TERMINUS & ONE END WITH A FREE CARBOXYL (COOH) GROUP: C-TERMINUS.
H BOND
THE ATTRACTION BETWEEN A H ATOM AND AN ELECTRONEGATIVE ATOM, SUCH AS NITROGEN OR OXYGEN.
(1/10th The strength of a covalent bond).
IONIC BOND
Between two close, oppositely charged
R groups (+VE & -VE).
DISULPHIDE BRIDGE
-S-S-
Covalent bond between 2 cysteine A.A’s.
Cysteine A.A have an R-Group with Sulphur in them
ENZYME
A PROTEIN THAT ACTS AS A BIOLOGICAL CATALYST AND SO LOWERS THE Ea WITHOUT BEING USED UP/CHANGED (no perm change in structure) ITSELF.
ACTIVE SITE
A SEQUENCE OF A.A THAT MAKES UP THE REGION OF AN ENZYME
INTO WHICH THE SUBSTRATE FITS
IN ORDER TO CATALYSE A REACTION.
COMPLEMENTARY
Having shapes or chemical properties that fit together precisely, allowing two molecules to bind specifically.
LOCK AND KEY:
ONLY THE CORRECTLY SIZED KEY (SUBSTRATE) FITS INTO THE KEYHOLE (ACTIVE SITE) OF THE LOCK (ENZYME).
ACTIVE SITE IS EXACT COMPLEMENTARU SHAPE AT OPTIMUM TEMP SO REACTIONS ARE FASTEST IN THESE CONDTIONS.
FOLLOWING THE REACTIONS, THE PRODUCTS DONT FIT IN THE ACTIVE SITE, SO THEY ESCAPE, LEAVING THE ENZYME UNALTERED AND FREE TO CATALYSE MORE SUBSTRATE.
LIMITATIONS INCLUDE THAT THIS SUGGESTS ENZYMES HAVE A RIGID STRUCTURE, BUT THIS IS UNTURE.
INHIBITOR
A SUBSTANCE WHICH REDUCES THE ACTIVITY OF AN ENZYME AND MAY BRING IT TO A HALT.
ISOMER
SAME MOLECULAR FORMULA, DIFFERENT STRUCTURE.
ESTER BOND
O=C-O JOINS FATTY ACID TO GLYCEROL
ORGANIC BASE
NITROGEN CONTAINING HETEROCYCLIC COMPOUNDS.
DNA - ATCG.
RNA- AUCG.
ATP
AN ACTIVATED NUCLEOTIDE FOUND IN ALL LIVING ORGANISMS, PRODUCED IN RESP AND ACTS AS AN ENERGY CARRIER.
LATENT HEAT OF VAPORISATION
Heat energy required to change liquid at BP to gas at same temperature.