Week 1 and 2 Handout Answers

Week 1 and 2 Handout Answers - BIBC 100 Mel Section A05...

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BIBC 100 – Mel – Section A05 Jonathan Goldstone – [email protected] OH: Thu 3:30-4:30pm, BioMed Library Week 1 Proteins Macromolecule made up of sequences of the 20 basic amino acids, which are joined in one long chain by peptide bonds, but are folded into their functional structure mainly by non-covalent interactions Hydrogen Bonding (Section 2.1 pg45) o Weak electrostatic interaction between an electronegative atom (N or O) and a hydrogen atom that is covalently linked another N or O o Make sure you can identify where two molecules can potentially form a hydrogen bond, practice using molecules such as the DNA bases Hydrophobic Interactions/Effect (Section 2.1 pg48) o The tendency for non-polar groups to associate with each other in an aqueous phase (like water). This effect is caused by the tendency of surrounding water molecules to seek their most favourable energy state o In sickle cell anemia, due to a point mutation of a Val substituting a Glu, this creates a point of hydrophobic attraction that causes mutated hemoglobin to stick together and aggregate into insoluble fibers Other Interactions (Table 2-5 pg50) o Ionic interactions, van der Waals interactions o You should know what those are Amino Acids (Section 3.1 pg75) Be really, really familiar with them (or just memorize them, that helps, too) Know which ones are polar, hydrophobic, charged, acidic/basic, aromatic Know what a Zwitter ion is (the ion ized form of an amino acid) Make sure you can draw an amino acid titration curve in your sleep o Know what pI , pK 1 , pK 2 , and pK R are, see Fig 3-10 pg79, Fig 3-12 pg81 Protein Structure Primary – amino acid residues Secondary – back bone interactions (basically α -helixes and β -sheets) Tertiary – side chain interactions
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BIBC 100 – Mel – Section A05 Jonathan Goldstone – [email protected] OH: Thu 3:30-4:30pm, BioMed Library Quaternary – subunit assembly Peptide bond undergoes resonance so it behaves similar to a rigid double bond o Therefore only certain degrees of movement allowed for amino acid residues, these are shown in a Ramachandran plot (pg117) KNOW THIS!!
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BIBC 100 – Mel – Section A05 Jonathan Goldstone – [email protected] OH: Thu 3:30-4:30pm, BioMed Library Questions Amino Acids: 1.
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