key words (biological molecules) AS

• adenosine triphosphate 


  the biological molecule that provides energy to drive cell processes.
• adenine


  a nitrogenous base, one of the components of ATP and nucleic acid nucelotides.
• ribose 


  a pentose sugar, common to nucleotides and ATP
• phosphate


  the phosphate group is the 3rd component of an ATP molecule and is where the energy is stored and released through hydrolysis
• adenosine diphosphate


  the product of hydrolysing ATP, can be condensed back to ATP to continue the cycle of energy absorption or release.
• photosynthesis


  the biochemical process by which plants use sunlight to harness energy
• photophosphorylation


  the biological process that forms part of photosynthesis where inorganic phosphate is added back to ADP through condensation
• respiration


  the process by which energy is released within cells of animals and plants
• nucleotide


  the monomer of nucleic acid
• pentose sugar


  sugar containing 5 carbons
• base


  the nitrogenous base is the identifying part of a nucleotide, can be adenine, thymine, uracil, guanine or cytosine.
• phosphate group


  another group that makes up a nucleotide, through the phosphate groups that nucleotides bond.
• phosphodiester bond 


  the bond formed through condensation reactions that links nucleotides together in polynucleotides.
• ribose (regards to RNA)


  the pentose sugar in the chains of RNA
• deoxyribose


  another pentose sugar that forms the back bone of DNA
• base pair 


  forms a long molecule of DNA and results from the specific features and hydrogen bonding between bases.
• complimentary bases


  the specific pairs that come together to form base pairs. adenine - thymine/uracil. cytosine - guanine.
• nuclear division


  the initial division of the nucleus and its contents before cell division occurs.
• cytokinesis 


  the final splitting of the cell to form 2 new cells.
• semi conservative replication


  a model by which we explain the replication of DNA, gets its name from the fact that the 2 resulting DNA molecules each have half of the original genetic info.
• DNA helicase


  the enzyme responsible for breaking the hydrogen bonds between bases to split a DNA molecule into individual polynucleotide strands.
• DNA polymerase


  an enzyme that reforms the new molecules by encouraging the attachment of free nucleotides.
• catalysts 


  molecules that reduce the activation energy of reactions, making them easier, quicker and reducing the enrgy needed for them to progress.
• activation energy


  the amount of initial energy needed for a reaction to profess to products.
• specificity 


  the fact that the target molecule or substrate for a given enzyme is specifc
• active site


  the functional part of the enzyme protein that attaches to the substrate
• substrate 


  the molecule on which the enzyme is designed to work.
• enzyme substrate complex


  the temporary molecule formed when the enzyme and substrate bond
• intermediate


  a molecule that exists temporarily during the course of a reaction, eg: the enzyme substrate complex.
• lock and key model


  an earlier model of enzyme action that likened the enzyme to a lock and the substrate to a key.
• induce fit model


  a more modern approach to enzyme action that accounts for the flexible nature of an enzymes structure,
• denaturation 


  occurs above a certain temperature, usually around 60C or extreme pHs and causes the substructure of a protein to come apart and for enzymes it makes the active site ineffective.
• optimum


  the best scenario. Optimum pH is the pH where the enzyme activity is highest. Optimum temp is the temp where the enzyme activity is highest.
• pH


  • log 10[H+]
• pH


  pH is scale that measures the concentration ion of solutions.
• enzyme inhibition 


  where the presence of another substance directly or indirectoy impacts the effectiveness of an enzyme.
• competitive inhibitors 


  the inhibition of enzymes by inhibitor molecules binding to the active site and reducing those available for the actual substrate.
• non-inhibitors 


  the inhibitions of enzymes by inhibitor molecules that bind to an alternative site on the enzyme but deform it changing the shape of the active site and preventing the substrate from binding.
• amino acid


  the sub unit of proteins/peptides. made of an amino group, carboxyl group and a unique R group that distinguish the 20 amino acids.
• amino group


  the amino group is the -NH2 part of an amino acid.