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F334
A2 salters mixture of descriptions and exam answers
Question | Answer |
---|---|
Atom Economy | The efficiency of a chemical process in terms of all atoms involved (desired products produced) |
Chiral | A carbon atom with four different functional groups that has a non-superposable mirror image |
Crystallinity | How polmer chains are packed together in an ordered way. |
Glass Temperature | The temperature when a polymer becomes brittle because the chains cannot move over each other so break when a force is applied. |
Melting Temperature | The temperature at which a polymer melts |
Intermolecular bond | are attractions between one molecule and a neighbouring molecule. |
Oxidation State | the degree of oxidation of an atom in a chemical compound |
Standard Electrode Potential | the potential difference between the electrode and and electrolyte(at 1 M), at standard conditions(1atm, 298K) |
Ionic Equation | a chemical equation for a reaction which lists only those species participating in the reaction. |
Electronegativity | The ability of an atom to attract electrons in a covalent bond. |
Ligand | an ion or molecule that forms a dative covalent bond with a metal ion. |
Bidentate | A ligand that binds through two sites. |
Coordination number | The number of dative covalent bonds that are formed with the central metal ion. |
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. |
Amino Acid | compounds made from amine and carboxylic acid functional groups, along with a side-chain specific to each amino acid. |
Primary Structure of Protine | the linear sequence of its amino acid structural units |
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. |
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 |
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. |
Clinical Trials | Is it safe? Does it work? Is it better than what's available? |
E/Z isomerism | Isomerisation which has a double bond with two priority functional groups on either side |
Enantiomers | Sterioisomers that are nonsuperimposable mirror images |
Co-Polymers | a polymer derived from two (or more) monomers. |