Draw the structure of the tripeptide Lys-Pro-Thr?

What are the term of anticodon loop?

Write a structural formula for a tetrapeptide composed of phenyl-alanine, glycine, aspartic acid, and histidine in which the phenylalanine is N-terminal and the histidine is C-terminal. How many different tetrapeptides could be written that fit the criteria in this question?

Draw the structure of the PTH derivative you would obtain by Edman degredation of the peptide: ALPF.

You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])

At what pH does peptide the His-Arg have a net charge of +1.7?

Refer to Problems 26.62 and 26.63. What dipeptide is synthesized from the informational DNA sequence T-A-C-C-C-T?

What is oligonucleotide adapter?

Polylysine adopts a random structure in solution at physiological pH (i.e. 7.4). Given that the e-amino group of lysine has a pKa of 10.5, under what circumstances do you think polylysine will form an a-helix? Give an explanation for your decision.   Given the pKa of the side-chain COOH group, under what circumstances would you anticipate polyglutamate to form an a-helix?

Proline is one of the amino acids in the "special" groups of sidechains. One reason for this is the dramatic impact it can have on secondary structure.  a) draw the lewis structure for a tripeptide with the sequence Ala-Pro-Ala b) Proline residues are rarely found in alpha helices - in fact, they are often referred to as helix-disrupting amino acids. Thinking about intermolecular interactions, provide an explanation for why proline might disrupt alpha-helices. c) Proline also has a similar effect on beta-sheets, and is rarely found in the middle of beta sheets. Thinking about noncovalent interactions, provide an explanation for why proline might disrupt beta-sheets.