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Unformatted text preview: Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM mercaptoethanol yields peaks for proteins of 34,000 and 26,000 molecular weight. Explain what can be determined about the structure of this protein from these data. 9) Which amino acids would be capable of forming H bonds with a lysine residue in a protein? 10) Poly –L-glutamate adopts an alpha helical structure at low pH but becomes a random coil above pH 5. Explain this behavior. ANSWERS 1) H bonding, hydrophobic interactions, Van der Waals forces, electrostatic interactions. 2) Primary – this is the amino acid sequence, secondary – residue by residue building of the backbone conformation, tertiary – the three dimensional conformation of a polypeptide or single protein chain, quarternary – the three dimensional structure of a multi-subunit protein. 3) proline – it puts a “kink” in the alpha helix due to restricted stearics of the structure 4) parallel beta sheets. 5) 6) 7) 9) 10)...
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This note was uploaded on 04/17/2011 for the course PHY 7b taught by Professor Taylor during the Winter '08 term at UC Davis.
- Winter '08