What bond type forms primary protein or peptide structure

Reference no: EM133650660

Questions

1. Give the one and three letter abbreviations and R group classification for:

Alanine, Cysteine, Proline, Phenylalanine, Lysine, and Aspartate

2. What bond type forms the primary protein or peptide structure? Where in the cell is this bond created?

3. What are the advantages and disadvantages of HPLC as a technique for the separation of proteins and peptides? Name one other technique one might employ for separating and purifying proteins.

4. Define the term PI as it relates to an amino acid.

5. Which degradation procedure provides information about the primary structure of proteins? Explain this process in detail.

6. What property of amino acids permits the measurement of protein concentration by UV light absorption?

7. Can the amino acid methionine perform the same function as cysteine? ? Explain in detail why or why not.

8. Explain why individual amino acids are soluble in water, and why not all peptides are water-soluble?

9. Name a critical reagent used in electrophoresis to separate polypeptides based on their mass.

10. How do number, sequence, and properties of amino acids in a protein affect its structure and function?

11. Using the UF library resources online, locate the following journal article:

Touch V, Hayakawa S, and Saitoh K. (2004) Food Chemistry 84 (3): 421-428.

Protein functions are dictated predominantly by their sequence and structures. Review the article above and briefly describe what changes the researchers imposed upon the protein lysozyme, how they accomplished this, and what effect those changes had on the properties and functions of that protein.

Reference no: EM133650660

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