4.3 Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.
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4.3 Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.
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- 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.Given the following Peptide: Q6 *H;N-Phe-Asp-Ala-Arg-Gy-His-Arg-Asp-Glu-His-Tyr-CO 6a. What is the peptide's net charge at pH 2.0, pH 6.0, pH 7.4, and pH 10.2? (show work) 6b. What is the approximate isoelectric point of this peptide?Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous solution at pH=10.3. (Relevant pKa values are: 2.2,4.3,6.0,9.8 and 10.1)
- Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.19.40 Indicate whether each of the following statements describes the primary, secondary, tertiary, or quaternary protein structure: a. Hydrophobic amino acid residues seeking a nonpolar envi- ronment move toward the inside of the folded protein. b. Hydrophilic amino acid residues move to the polar aqueous environment outside the protein. c. An active protein contains four tertiary subunits. d. In sickle cell anemia, valine replaces glutamate in the B-chain.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.
- A protein gives, under conditions of buffer composition, pH, and temperaturethat are close to physiological conditions, a molecular weight by size exclusion measurements of 140,000 g/mol. When the same protein is studiedby SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits, and the kinds of bonding(covalent, noncovalent) existing between subunits.Amino acid structure For any ionizable group, indicate the pka value and draw the structure that would be expected at the pH inside the cell (~7.4).1.3 pH-Dependent Change of Conformation of Poly-L-glutamic Acid A synthetic polypeptide made up of L-glutamic acid residues is in a random coil configuration at pH 7.0 but changes to a helical when the pH is lowered to 2.0. Explain this pH-dependent conformational transition.
- Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.Given the following peptides below, what would be more soluble at the indicated pH? 1. (Gly)20 or (Glu)20 in pH 7.0 2. (Lys-Ala)3 or (Phe-Met)3 in pH 7.0 3. (Gly)20 or (Glu)20 in pH 6.0|| 4. (Ala-Ser-Gly)s or (Asn-Ser-His)s in pH 6.0 5. (Ala-Asp-Gly)8 or (Asn-Ser-His)8 in pH 3.0The major difference between a protein molecule in its native state and inits denatured state lies in the number of conformations available. To a firstapproximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.(a) For a protein of 100 residues, estimate the entropy change per moleupon denaturation.(b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?(c) Will the fraction denatured increase or decrease with increasingtemperature?