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12 Cards in this Set
- Front
- Back
• Outline the reaction by which amino acids are joined together.
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Condensation reaction. COOH and NH2
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• Sketch a trimeric peptide, illustrating the amino -terminus, carboxyl terminus and side chains.
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Need image.
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• Give examples of the post-translation modifications of amino acids, with reference to glycosylation, hydroxylation and carboxylation.
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o Hydroxylation:
Proline becomes hydroxy-proline: collagen fibres The extra hydroxyl helps stabilise (vit C, scurvy) o Glycosylation Sugars are added to asparagine residues of protein (look into this ?) Makes them more soluble/prevents degradation o Carboxylation Glutatamate gamma-carboxyglutamate Essential to clotting cascade (warfarin inhibits) |
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• Understand the concepts of primary structure, secondary structure, tertiary structure & quaternary structure with respect to proteins.
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o Don’t forget domains
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• Distinguish between an α-helix and a β-pleated sheet and appreciate the bonds that stabilise their formation.
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o Hydrogen bonds stabilise helices and pleated sheets.
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• Appreciate the different types of bond that combine to stabilise a particular protein conformation.
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o Disulphide Bridges
Covalent bonds Occur when cysteine side chains are “oxidised”? Makes a covalent link between two amino acids o Hydrogen Bonds, of course o Ionic Interactions Due to electrostatic attractions between charged side chains Relatively strong (especially if in hydrophobic interior) o Van der Waals o Hydrophobic interactions Major driving force |
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o Ionic Interactions
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Due to electrostatic attractions between charged side chains
Relatively strong (especially if in hydrophobic interior) |
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1st law of thermodynamics
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Energy can neither be created nor destroyed; only transferred/formed/etc
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2nd law of Thermodynamics
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o 2nd: In any isolated system, disorder can only increase (entropy)
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• Describe how oxidation and reduction involve the transfer of electrons
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Redox potentials/etc. Hydrogen half-cell/etc
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• Explain the concept of free energy and how we can use changes in free energy to predict the outcome of a reaction.
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o Free energy is the amount of energy in a molecule that could perform useful work at a constant temperature. Measures entropy/enthalpy
If Gibbs is negative, reaction will be spontaneous |
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• Draw the chemical structure of ATP and explain how it acts as a carrier of free energy and is used to couple energetically unfavourable reactions
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o Its energetically favourable reaction coupled to an unfavourable reaction can make an overall favourable one. So long as overall gibbs is negative.
o ATP to ADP is very favourable (-31kjmol-1) |