Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ?(Select all that apply.)The two peptides have different compositions.The two peptides have different isoelectric points.The two peptides have different titration curves.The two peptides differ in amino acid sequence.[References]If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced byanother amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group?(Select all that apply.)Both of the carboxyl groups are deprotonated.The amino acid-carries a negative 2 charge.The amino acid carries a negative 4 charge.The amino groups are in the form -NH".Both of the amino groups are deprotonated.

Amino acids are biomolecules in which an amino group and a carboxyl group are linked to the same…

Answered: Consider the peptides…

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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Peptide A: AFEQHSR Calculate the isoelectric point of Peptide A using the pKa values in Table 4-1 of Voet, Voet and Pratt. Assume that the pKa values for the N-terminal amino group and C- terminal carboxyl groups are 8.0 and 3.5, as previously discussed in class. 3.785 5.055 7.02 10.24 3.50
Draw the polypeptide T-R-I-P at pH of 7. Label each residue with the 3-letter code, label the N- and C-termini. What is the isoelectric point of this peptide?
Given the following sequence present within a large, soluble, globular protein: N-Asn Tyr Ser His Gly Asp Arg Tyr Thr lle Leu Leu Met Glu His Glu Phe Ile Val Pro Gly Pro Phe Thr Val Glu Val Asn -C What secondary structural elements are most likely present in this sequence? Please annotate the sequence to show where these structures begin and end.
Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
Identify and briefly describe the different PEGylation strategies you can use to PEGylate this peptide and draw the chemical structure of the resulting mPEG peptide conjugates.
On the paper provided, draw the chemical structure of a peptide with a sequence LEMD at pH 7. The pKa values for the amino acid sidechain of E and D are 4.1 and 3.9, respectively.
Are phosphate groups considered negatively charged and acidic (because the negative charge is due to deprotonation at cellular pH)? Overall, I am confused about the different categorizations for functional groups. My understanding is there are acidic and basic functional groups (for polar, charged amino acids) and there are positive, negative, and neutral functional groups. Is this correct? If so, how do we determine how to categorize functional groups/amino acids in this manner?
Hair is comprised largely of keratin, a fibrous protein consisting of two a-helices wrapped around each other in a left-handed coiled-coil. The diagram below compares a partial alignment of the amino acid sequences of a form of human keratin and of ovine keratin. For each pair of dissimilar aligned amino acids, (i) indicate if a side chain is associated with a discrete charge by writing or (at pH 7) adjacent to the letter; and (ii) indicate whether each amino acid is polar (p) or apolar (a) in the case of aligned, electrostatically-neutral, side chains. In the diagram, 219 and 158 designate se-quence positions of the first aligned residue in each polypeptide strand. human II 5 219 ovine II 7c 158 FEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAE FEGYIETLRREAECVEADSGRLSSELNHVQEVLEGYKKKYEQEVALRATAE
Provide the number of polypeptide chains present andthe number of amino acid residues in each chain. for https://www.rcsb.org/structure/6j20 Provide the molecular weight of the protein orprotein complex and the total number of atoms. (All of this information can be found in the PDBpage.) Create a figure (available in the PDB page) that shows the topology of your protein, i.e.the secondary structures adopted by different regions of the protein (alpha helix, beta strand).Make sure to also provide a figure legend that helps interpret the figure and appropriate figurecaption that briefly explains the figure.
you have isolated the following peptide: His-Ser-Arg- Ala-Glu- Leu- Pro- Gly Calculate the approximate charge of the peptide at Ph 1, 3, 5, 8, 11, 14 AND what is the PI of this peptide?
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
A) Can you please tell me which of these A.A have a negative side chain? Names of choices in picture provided. B) Can you please tell me which A.A have a hydrophobic side chain and why? Names and choices in picture provided. Thank You so much!!

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