Consider the following peptide: alanyl-glutamyl-lysyl-cysteyl-asparagine.1- Write the semi-developed formula of this peptide at pH = 1. Indicate the N-terminal and C-terminal ends of the peptide. Indicate the carbones a.2- This peptide comprises 5 ionisable groups whose pKa values are, respectively:2 ; 4.3 ; 8.3 ; 9.7 ; 10.5. Attribute a pKa value to each ionisable group. Justify your answeranswer (using the Table, p. 8 when necessary).

The given peptide is comprised of 5 amino acids. In order to write the name of a peptide , we add…

Answered: Consider the following peptide:…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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a) Where is the N-terminus of this peptide? Left Middle Right b) What type of secondary structure is the majority of this structure? loops alpha helix Beta sheet unstructured c) The X's indicate the alpha carbons of residues 10, 13, and 17 (labeled in the sequence above). Where would you expect this part of the structure to be found in the tertiary structure of the protein? Briefly explain your reasoning. d) The dashed line in black is indicating an interaction that is present within this structure. Draw this interaction, including all the atoms necessary for this interaction to occur. Label any partial charges present in your drawing. please upload the drawing.
A fragment of a protein commonly found in food was sequenced and found to have the sequence: RDCEHKY Draw the structure, showing the form expected to be dominant at a physiological pH (7.4). Discuss how changing the pH will affect the fragment, and what implications this has on the overall structure of the protein. What is the difference between the sequence above and the sequence YKHECDR?
What is the isoelectric point of the following peptide molecule? Asp-His-Glu-Gly-Lys-Tyr-Leu-Phe-Arg-Ser-Cys Relevant pKa values are; 2.2, 3.8, 4.3, 6.0, 8.3, 9.8, 10.1, 10.5, 12.5 and 13.1 3.0 9.1 7.2 5.2 4.1 ONLY one correct answer
Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.
Draw the structural formula of the oligopeptide if the amino acids are arginine, glutamine, glycine, methionine and glutamic acid considering the first amino acid is the N-terminus
At which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17
The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributions from form I. Why? (b) Calculate the average charge on arginine when pH = 9.20. (c) Is the value of average charge you calculated in part b reasonable, given the pI you calculated in part a? Explain your answer
A peptide with 12 amino acids has the composition (not sequence) Asp 2Cys 2Glu 2Leu 2Ser 2Tyr Val. It also has Ser as the N-terminal residue and Cys as C-terminal. Partial acid hydrolysis gave these peptide sequences: (a) SerLeuTyr (b) TyrCys (c) LeuTyrGlu (d) GluLeuGlu (e) SerValCys (f) CysSerVal (g) GluAspTyr . What is the peptide sequence?
What charge is carried by the peptide FREEENERGY at pH 7? (pKas: N-terminus: 9; C-terminus: 3; Arginine 11.6; Glutamic acid, 4.3)
Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
At what pH can you separate the following peptides: ala-ala-ala, glu-glu-glu, his-his-his? OA 2.0 B. 4.0 C. 5.0 O D. 7.0 E. 9.5

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