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A2 salters mixture of descriptions and exam answers

Quiz yourself by thinking what should be in each of the black spaces below before clicking on it to display the answer.
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Question
Answer
Atom Economy   The efficiency of a chemical process in terms of all atoms involved (desired products produced)  
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Chiral   A carbon atom with four different functional groups that has a non-superposable mirror image  
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Crystallinity   How polmer chains are packed together in an ordered way.  
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Glass Temperature   The temperature when a polymer becomes brittle because the chains cannot move over each other so break when a force is applied.  
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Melting Temperature   The temperature at which a polymer melts  
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Intermolecular bond   are attractions between one molecule and a neighbouring molecule.  
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Oxidation State   the degree of oxidation of an atom in a chemical compound  
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Standard Electrode Potential   the potential difference between the electrode and and electrolyte(at 1 M), at standard conditions(1atm, 298K)  
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Ionic Equation   a chemical equation for a reaction which lists only those species participating in the reaction.  
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Electronegativity   The ability of an atom to attract electrons in a covalent bond.  
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Ligand   an ion or molecule that forms a dative covalent bond with a metal ion.  
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Bidentate   A ligand that binds through two sites.  
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Coordination number   The number of dative covalent bonds that are formed with the central metal ion.  
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Sterioisomers   molecules that have the same molecular formula and sequence of bonded atoms, but that differ only in the three-dimensional orientations of their atoms in space.  
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Amino Acid   compounds made from amine and carboxylic acid functional groups, along with a side-chain specific to each amino acid.  
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Primary Structure of Protine   the linear sequence of its amino acid structural units  
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Secondary Structure of Protine   The peptide linkscan form hydrogen bonds with each other meaning the chain isn't a straight line. Alpha helix or Beta sheet.  
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Tertiary Structure of Protine   The chain of amino acids is itself often coiled and folded in a characteristic way that identifies the protine. Extra bonds can form between different parts of the polypeptide chain, which give the protine a three-dimentional shape  
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Thin-Layer chromatography   Draw a pencil line near the bottom of the plate and place 1 drop of each solvent on the line. Place plate in solvent line above the solvent level and add lid. When solvent nears the top of the plate reove plate. Locate spots with UV light or iodine.  
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Clinical Trials   Is it safe? Does it work? Is it better than what's available?  
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E/Z isomerism   Isomerisation which has a double bond with two priority functional groups on either side  
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Enantiomers   Sterioisomers that are nonsuperimposable mirror images  
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Co-Polymers   a polymer derived from two (or more) monomers.  
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Created by: Tyranacid
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