What is the net charge on the amino acid cysteine at pH 8.0? (pKa values are α-carboxyl 2; α-amino 10; side chain 8)
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Hi, please help with this question:
What is the net charge on the amino acid cysteine at pH 8.0? (pKa values are α-carboxyl 2; α-amino 10; side chain 8)
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- Predict the direction of migration for the following amino acids in solutions of the specified pH. Write Isoelectric, if no migration occurs: Lys at pH=12 (pk values: 2.2; 9.2; 10.8) Glu at pH= 2.0 (pk values: 2.1; 9.5; 4.1) Leu at pH= 6.0 (pk vaues: 2.3; 9.7)please help me understand asap Please draw by hand a tripeptide of Glu, Gln, and 1 amino acid of your choice (Not Glu or Gln again) at pH 7.0 and 9.0. The only requirement is that the amino acid should be 1 of the amino acids with ionizable R groups. Peptide should have appropriate charges on groups. PleaseNeed help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thr
- peptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.Determine the net charge (to the nearest integer) on the following peptide at pH 5 AND pH 12. Estimate the isoelectric point (pl) for this peptide: H2N-Leu-Gly-Lys-Glu-COOH Assume the pK,s for functional groups are: alpha-amino 6. alpha-carboxy sidechain-amino (Lys) 10.5 sidechain-carboxy (Glu) 4.2 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =6.6 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =3.1 O Net charge at plH 5 and 12 is +2 and -1, respectively, pl =7.5 O Nct charge at pH 5 and 12 is +1 and -1. respectively,. pl -4.5 2.A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.
- What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.R V. Phospholipids are the main structural lipids that comprise cellular and organellar membranes. One abundant phospholipid in bacterial cell membranes is phosphatidylethanolamine (PE), which has a generic structure shown on the right. Note that R1 R and R2 are representative alkyl chains of attached fatty acids, each having about 16 – 20 carbon atoms. a) The overall net charge in one PE molecule is: -2 -1 0 +1 +2 CH₂ Phosphatidylethanolamine (PE) -CH H₂C. b) The glycerophosphate backbone in PE is a: D-enantiomer c) The fatty acids are attached to PE via which type of bond? amine L-enantiomer racemic NH3 amide ester ether d) Draw the commonly used cartoon representation of one phospholipid molecule. Label the hydrophilic and hydrophobic parts.Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively charged at pH 7. Polar and neutral aspartate H Ser H₂N-C-CH₂-C-COO NH3 lysine Leu Nonpolar Answer Bank H OOC-CH₂-CH₂-C-COO NH3 Positively charged H CH₂-C-COO NH3 hydrophobic amino acids Negatively charged
- The isoelectric point, pI, of the protein deoxyribonuclease I is 10.2 , while that of pepsin is 1. What is the net charge of deoxyribonuclease I at pH 7.3 ? What is the net charge of pepsin at pH 3.5 ? The isoelectric point of tryptophan is 5.89 ; phenylalanine , 5.48 . During paper electrophoresis at pH 6.5 , toward which clectrode does tryptophan migrate? During paper electrophoresis at pH 4.5, toward which electrode does phenylalanine migrate? [Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has, values of 2.4 (carboxyl group) and 9.7 (amino group). Isoleucine at pH 7 Isoleucine at pH 1 CH3 CH₂ + H₂C CH +H₂N- C H Incorrect Isoleucine at pH 13 Incorrect H₂C H₂N- CH₂ | CH₂ CH c- C H 0 ĭ Incorrect H₂C +H₂N-Calculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr