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Allosteric enzymes
Enzymes that change the conformation in response to the modulator
Alpha helix
Polypeptide chain coiled into a helix with hydrogen bonds to stabilise
Alternative RNA splicing
Removal of non-coding introns from primary mRNA transcript to leave only the coding exons ( several different combinations)
Beta pleated sheets
Polypeptide chains arranged in rows with the chain folding in parallel or anti-parallel arrangements
Conformations
Structural arrangements of the polypeptide within a protein; it can be altered by factors such as PH
Co-operativity
Changes in the binding of a target molecule to one subunit of a multiunit polypeptide changes the affinity of the other subunits for the target molecule
Disulfide bridge
A strong covalent bonds that stabilises the tertiary and quaternary structures of many proteins
Endoplasmic reticulum
A network of membrane tubes within the cytoplasm of a eukaryotic cell
Exon
A section of the DNA retained during splicing
Glycoprotein
A protein with a carbohydrate added by a post translational modification
Golgi apparatus
A series of flattened membrane discs that package proteins into membrane bound vesicles inside the cell before the vesicles are sent to their destination
Hydrogen bonds
Attractions between polar in which hydrogen is bound to a larger atom
Hydrolases
A class of enzyme that use water to break chemical bonds
Introns
A section of RNA usually removed during splicing
Ionic bonds
A type of bonding that involves electrostatic attraction between oppositely charged ions
Ligand
A substance that can bind to a protein; the protein has a shape complimentary to the ligand to allow binding
Lysome
A modified Golgi vesicle containing hydrolytic enzymes
Modulators
These bind to a secondary site on an enzyme to alter its conformation; positive modulators activate enzymes and negative modulators deactivate
Monomers
A mollecule that can bind chemically to other monomers to form polymer
Non-coding RNA gene
A gene that codes for RNAs other than messenger RNA , so do not encode protein
Phospholipid
A component of cell membranes
Post translational modification
Adittion of different chemicals groups to, or modification of, a protein to alllow a particular function
Prosthetic group
A non-protein groups unit tightly bound to a protein necessary for its function
Protein kinases
Catalyse the transfer of a phosphate from a donor mollecule
Protein Phosphatases
An enzyme that removes a phosphate group from its substrate
Primary structure
Sequence in which amino acids are found joined by peptide bonds within a protein
Secondary structure
Hydrogen bonding occurring within a polypeptide forming alpha helices or beta- pleated sheets
Tertiary structure
Bonding of many types occurring between the R-groups of amino acids within a protein
Quaternary group
The arrangement of multiple folded polypeptide units folded together
Proteolytic cleavage
A major form of post translational modification; it occurs when a protease cleaves one or more bonds in a target proteins to activate, inhibit, or destroy
Proteome
The entire set of proteins expressed by a genome ( larger than the genome)
R-groups
Side groups that allow different bonding between amino acids and give them their wide range of functions
Basic R-group
Contains an amine functional group, producing a basic solution
Acidic R-group
Contains an acid in functional group and produces an acidic solution
Polar r-group
Group that prefers to exist in a watery environment
Hydrophobic r-group
Composed mostly of Hydrogen and carbon, and then to be repelled from water
Rough endoplasmic reticulum
Organelle made up of membranes with ribosomes attached
Signal sequence
A short sequence of amino acids at one end of the poly peptide that determines its location within the cell
Smooth endoplasmic reticulum
A membrous organelle found is most euakrotyic cells; its main function are synthesis of lipids and steroid hormones
Turns
Secondary structures that reverses the direction of the poly peptide chain
Vesicles
Small membrane bound compartments filled with liquid