Given below is a sequence of a polypeptide: AVLLRKIFWFDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pKa C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Сys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule below pH 3.5? [Select] What is the total charge of this molecule at pH 5? [Select ]
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- Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys CysGiven below is a sequence of a polypeptide: AVLLRKIFWFDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pka C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 11? [ Select ] What is the total charge of this molecule at pH 13? [ Select ] What is the isolectric point for this molecule? (Select]The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
- What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K-R-W at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K (pКa %3D 10.5) O +2 O-1 O +1based on this oligopeptide (KEQSCMV) would someone be able to help me on the following questions? What moieties within oligopeptide are those mainly responsible for the formation of an alpha-helix? Name the process that leads to the unfolding of the alpha helix to yield a random coil. State and justify, for oligopeptide, which amino acid side chains will be involved in: hydrophilic interactions, hydrophobic interactions, disulphide bridges and salt bridges. In each case, briefly justify your choice.The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds
- 8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K (pKa = %3D %3D %3D %3D 10.5) O +2 O+1 O-1 00The primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]
- Below is the primary structure of a protein. A R 1 I I H H || O H 1 Psi bond [Select] Phi bond [Select] N-terminus [Select] B C D H O I || C-terminus [Select] NC-C-N-C-C-N-C-C-N-C-C-N-C-C - N... I 1 H H I R R H I 11 O HO I || R R I I H a. For each part of the question, select the letter associated the with appropriate component of the structure. Peptide bond [Select] I H U MO b. Which letter represents a bond without 360-degree rotation? [Select] H |Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser noneYou are studying a novel amino acid. It has an alpha-amino and an alpha-carboxylic group, and an ionizable side chain that carries a carboxylic group. A titration curve is shown below. Net charge a CD f 0 1 2 3 4 5 +1 [Select] 0 [Select] 6 7 pH Choose the letter that corresponds to the following charges on this novel acid. +2 [Select] -0.5 [ [Select] -1 [Select] 8 -2 [Select] I 9 10 11 12 13