L0 Styles Styles , ch , Pane 10. Which amino acids can participate in hydrogen b
ID: 140584 • Letter: L
Question
L0 Styles Styles , ch , Pane 10. Which amino acids can participate in hydrogen bonds? 11. All amino acids incorporated into proteins at the ribosome have what stereochemistry? Why do they all have this stereochemistry? 13. Look at figures 4-14 and 4-15 on pages 88-89. What amino acids are these structures derivatives of? 14. Explain the function and importance of glutathione. 15. What factors set the upper and lower limits for size of a protein? 16. Explain why pH and temperature must be controlled when purifying a protein. 17. Explain how ELIZAs, salting out, and the different types of chromatography work. Be able to devise a purification plan for a hypothetical protein. 18. How does 2D electrophoresis differ from sDS-PAGE and how do they each work to separate molecules? 19. How does ultracentrifugation work? 0. Explain the process of protein sequencing via Edman Degradation. Why must you first cleave the protein intoExplanation / Answer
Answer for question no. 10)
The amino acids serine, threonine, and tyrosine all have hydroxyl groups, which are classic hydrogen-bond donors. Asparagine and glutamine each have an amide group, which can participate in hydrogen bonding. Histidine and cysteine are both versatile amino acids.
Answer for question no. 11)
The amino acids are all chiral, with the exception of glycine, whose side chain is H. As with lipids, biochemists use the L and D nomenclature. All naturally occurring proteins from all living organisms consist of L amino acids. The absolute stereochemistry is related to L-glyceraldehyde, as was the case for triacylglycerides and phospholipids. Most naturally occurring chiral amino acids are S, with the exception of cysteine. The absolute configuration of the amino acids can be shown with the H pointed to the rear, the COOH groups pointing out to the left, the R group to the right, and the NH3 group upwards.
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