A. if a protein had two aspartic acid R groups interacting at pH 2, what kind of interaction would you see in its tertiary structure?
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- . Consider the structure of the amino acid aspartic acid. Indicate the hybridization about each interior atom. H HChoose Two. The Ramachandran plot indicates: B H Ca ||||||| Ⓒ. The C1 I A. Combined preference about both H しょしい O conformation preference for a C1-C² and c²_N bonde Existence of a peptide in an a-helical conformation Or P sheeted The prefered conformation about Can bond. The prefered conformation about C1-C² bond The prefesed conformation about peptide bond.A. 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.
- Peptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?a. Suppose that the R group of a histidine residue in a protein in its native tertiary structure is buried in the interior of the protein and is involved in a salt bridge (ionic interaction) with an oppositely charged residue. Unfolding the protein exposes both of the charged groups to water. Would you expect the pKa of the His R group (side chain) in the native protein to be a) higher or b) lower than the pKa of the same residue in the unfolded protein? Why? b. Is the exocyclic NH2 in cytosine acidic or basic? Why? NH, `N'. Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil conforma- tions will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.
- 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.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.BIOCHEMISTRY If the protein is more hydrophobic, then adding additional charge is not the best strategy. What are other excipients we might select instead of NaCl to try to interrupt these interactions?
- ɡive me example about the arranɡements of heptapeptide such as Arɡ, Phe, Val and etc.Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.Proteins are quite stable. The lifetime of a peptide bond in aqueous solution is nearly 1000 years. However, the free energy of hydrolysis of proteins is negative and quite large. How can you account for the stability of the peptide bond in light of the fact that hydrolysis releases much energy?