What amino acid side chains can be modified by methyl groups? What is unusual about methyl group addition compared to phosphate and acetyl addition to proteins?
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What amino acid side chains can be modified by methyl groups? What is unusual about methyl group addition compared to phosphate and acetyl addition to proteins?
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- 1. Draw the structure of Phe-Ser-Met-Glu, and indicate where the peptide bonds are.6. Peptide bonds link many amino acids into chains of subunits that make polypeptides, or proteins. In the space below, or on a blank sheet of paper, draw the dehydration synthesis reaction showing the peptide bond that forms between two alanine (C3H;NO2) amino acids. Remember that all amino acids have an amino functional group at one end (N-terminal end) and a carboxyl functional group at the other end (C-terminal end). Also, alanine is an amino acid that has a CH3 off the middle ("R" group) carbon.1. Show the Dehydration Synthesis reaction that occurs to form a dipeptide containing the following amino acids: i) cysteine and serine leucine and lysine
- 1. What is an amino acid that has aromatic heterocyclic side chain?11. Which of the following correctly illustrates a dipeptide and an amino acid in the optimal position to form a tripeptide? (A) R H H-N-C C-N-C Н— N— С OH OH н н H H H. (В) (R® (R R C-N- N Но OH HO OH H. H. H. (C) R H H. Н— N— С C С —С —N — H Н— N— С С—Н H. H. H. H. H (D) R H (R) C-N С—С —N —H Н— С —С HOʻ н н H. H H 0=U4. Which amino acids do not react to produce a purple color with ninhydrin. Why?
- 1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin.1. Draw the structures of two dipeptides: aspartic acid-glutamine and methionine-isoleucine with NH₂ and COOH at the amine and carboxylic acid ends. Show the abbreviations for both dipeptides using three-letter abbreviations and 1-letter abbreviations for the amino acid residues.
- 4. What is the net charge (approximately) on the polypeptide shown below at pH 12.5? Lys - Arg - Val-Cys - Glu1. To determine the sequence of amino acids in protein, partial hydrolyses at different points are made and then compared to other sets of partial hydrolyses For example: Complete hydrolysis gave: Phenylalanine-1 Histidine-2 Glutamic acid-1 Leucine - 4 Asparagine-1 Cystine -2 Glutamine-1 Glycine - 2 The Partial Hydrolyses yielded the following: 1st Hydrolysis : 4 polypeptides ● . IA: phe-val-asn-gln-his-leu IB: IC: leu-tyr-leu-val ID: val-cys-gly 2nd Hydrolysis: 3 polypeptides IIA: phe-val-asn-gIn-his-leu-cys-gly-ser-his-leu IIB: val-glu-ala-leu-tyr-leu IIC: val-cys-gly Write down the primary structure of this polypeptide by finding the overlaps of the amino acids therein: Serine-1 Valine-3 Alanine-1 tyrosine-1 cys-gly-ser-his-leu-val-glu-ala2. Show the Dehydration Synthesis reaction that occurs to form a tripeptide containing the following amino acids: valine, glycine and alanine