This preview shows page 1. Sign up to view the full content.
Unformatted text preview: C) proteins attracting primarily salt anions D) realing hydrophobic proteins from nonpolar tissue environments E) hydration of salt ions reducing solubility of proteins 3. A mixture of lysine and aspartic acid is applied to an anion exchange column at pH 7.5. Which amino acid will bind the column? Explain why. 4. Trypsin degradation of a peptide yields the fragments H, MNK, IMR and LMP. Cyanogen bromide treatment yields RH, RM, NKIM and LM. Deduce the sequence of the peptide. 5. It takes a minimum of about 40 amino acid residues for a polypeptide to fold into a stable structure. Explain what a stable structure means. Why does it take ~40 resides to form a stable structure? 6. The different polypeptide chains in a protein are known as------- (fill in the blank). Why do some proteins contain multiple polypeptide chains?...
View Full Document
This note was uploaded on 01/31/2010 for the course CHEM chem 114A taught by Professor Gourisankarghosh during the Fall '06 term at UCSD.
- Fall '06