BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
1st Edition
ISBN: 9780134172507
Author: APPLING
Publisher: Pearson Education
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Chapter 5, Problem 2P
Draw the structure of the peptide DTLH, showing the backbone and side-chain atoms.
a. Draw a water molecule making a hydrogen bond to a side chain H-bond donor.
b. Draw a water molecule making a hydrogen bond to a main chain H-bond acceptor.
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Given the peptide Lys-Glu-Trp
a) Draw the appropriate titration curve for this peptide. Label X and Y axis
b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net charge
Consider the following molecule.
a. Name it.b. Use the three-letter symbols for the amino acids torepresent this molecule.
Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.
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BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- a. A tetrapeptide is abbreviated as PSQE. Write the name of the amino acid at the N-terminal end. b. A tetrapeptide is abbreviated as FRWL. Write the name of the amino acid at the C-terminal end.arrow_forwardFor the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues b. What is the charge of the peptide at pH 7.0. Assign the following pKa values: 3,4,6,8,9 c. What is the pI of the peptidearrow_forwardA small protein has a sequence ACNCKAAPMLCARYCAMLH. The structure of this single peptide is stabilized by the formation of two separate disulfide bonds, but the locations of those disulfide bonds are unknown. In order to determine the location, you purify this peptide and treat it with trypsin (cleaves peptide bond at long, positively-charged side chains). Tryptic digestion generated two peptides. Based on this result, determine the location of the –S-S– bonds. Show them in a diagram on the sequence by connecting the corresponding residues. Explain your reasoning.arrow_forward
- Suppose that the sequence is part of a larger globular protein. Consider the probable location, either on the external surface or the interior of the protein, of each of the amino acid residues. The table gives the hydropathy index values for selected amino acids in the peptide. Amino acid Hydropathy index alanine 1.8 isoleucine 4.5 threonine -0.7 glutamine -3.5 lysine -3.9 aspartate -3.5arrow_forwardConsider the peptide with amino acid sequence NICE. Write the full name and the three-letter abbreviations of the amino acids in the peptide.arrow_forwarda. Draw the peptide chain (indicate if it is solid or hatched wedges) for the following: Glycine-(L)-Arginine-(D)-Proline-(L)-Glutamic Acid b. Compute for the isoelectric point. Show solution.arrow_forward
- draw a “trans” and a “cis” peptide bond of alanine and threonine with the peptide bond lying in the plane of the paper. Draw a second view of each peptide bonds now looking down/along the peptide bond (i.e. one atom of the peptide bond will be in front and will obscure the second one behind it). Using a circular arrow, demonstrate how the torsion angle can be directly “read” from the picture. You can do this with an accuracy of ~10°. Provide an explanatory caption.arrow_forwarda. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.arrow_forwardA. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.arrow_forward
- Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Valarrow_forwardConsider the peptide with amino acid sequence NICE. a. Write the full name and the three-letter abbreviations of the amino acids in the peptide. b. Calculate the net charge of the peptide at pH 7.0. Show you work in a table. c. Calculate the pI of the peptide. Show you work in a table.arrow_forwardPlease provide the amino acid sequence for both of the following protein usingarrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY