**Sickle Cell Hemoglobin and Hydrophobic Patches****Question:**Which amino acid pair constitutes the hydrophobic patch on sickle cell hemoglobin that results in the formation of protein oligomers with the Glu 6 --> Val 6 sickle cell mutation? Does normal hemoglobin contain this same amino acid pair constituting a hydrophobic patch?**Options:**1. ○ Phe 85 / Leu 88; no2. ○ Phe 85 / Leu 88; yes3. ○ Trp 85 / Leu 88; yes4. ○ Ile 85 / Leu 88; yes5. ○ Pro 85 / Lys 88; no

Sickle cell disease is caused due to inversion of one base pair (A -> T). Due to which, the sixth…

Answered: Which amino acid pair constitutes the…

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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You have discovered a novel protein that has a pl = 5.5. To study the functional properties of this new protein your research group has made a mutant that contains two amino acid changes-namely, a surface Phe residue in the normal protein has been replace by His (side chain pk = 6.1), and a surface Gln has been replace by Glu (side chain pk. = 6.0). The pl of the mutant protein is predicted to be: A. Greater than the pl of the normal protein. B. Less than the pl of the normal protein. C. The same as the pl of the normal protein.
Sickle cell anemia is a horrific molecular disease that causes a multitude of issues within the human body, despite the disease’s hemoglobin only slightly varying in structure, as normal hemoglobin’s glutamic acid is instead replaced with valine in the beta-globin amino acid chain. By only changing structurally in this slight amount , sickle cell takes on its unique shape which then causes a multitude of issues within the human body. How does the replacement of glutamic acid with valine end up resulting in this shape, and how would it affect its interaction with the rest of the body?
Titration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration reaction occurring at pK1 (pK1 = %3D 2.34)? O-NH2 + COH →-NH + H2O O-COOH + OH →-CO + H20 -COOH + -NH2 → -COO" + -NH2+ -CoO +-NH2* → -COOH +-NH2 O -NH3* + OH →-NH2 + H2O
What does this statement mean: "Upon folding of a protein many main chain amides replace their hydrogen bonds to water for those with other amide bonds" Is this true for alpha helix in proline racemase? and is there a pattern?
Consider an amino acid sequence: D1-G2-M3-E4-C5-A5-F7-H8-R9-I10-A11-H12-T13-Y14-G15-F16-P17-E18-A19-A20-M21-C22-K23-W24-E25-A26-Q27-P28 The β-turn structure is likely found at (Write down the residue number). A possible disulfide bond is formed between the residues and . The total number of basic residues are The addition of chymotrypsin will result in blank peptide fragment(s). The addition of trypsin will result in blank peptide fragment(s). The addition of CNBr will result in blank peptide fragment(s).
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hill coefficient
The hemoglobin in the fetus (HbF) is a structural variant of the hemoglobin in the mother (HbA). HbA is a tetrameric protein complex consisting of two α-globin and two β-globin subunits. HbF is made up of two αglobin and two γ-globin subunits, where the γ-globins are similar to the β-globins but γglobins have lower affinity for 2,3- bisphosphoglycerate or BPG. Studies of oxygen transport in pregnant mammals show that the oxygen-saturation curves between the red blood cells of the fetus and the mother are markedly different. 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding curves, determine the dissociation constant (Kd) for each hemoglobin complex. (Show correct units.) Kd of HbF + BPG: ________________ Kd of HbA + BPG: _____________________ b) Which has a higher affinity for oxygen? HbF+BPG HbA+BPG 3. a) How many BPG molecule(s) is/are expected to bind one hemoglobin complex? 1 2 3 4 b) BPG binding preferentially stabilizes which state…
is it true that aplha and beta are made up of same amino acids but Beta chain is longer than alpha chain？what is other difference and similarity？is the amino aicd sequence exactly the same as well？are their structure the same ？
When protein cannot precipitate out under the conditions for making tofu and cheese because (i) polar groups are highly abundant in the surfaces of whey proteins; and (ii) disulfide bonds are commonly present in the structures of whey proteins. Explain briefly why highly abundant polar groups and disulfide bonds could make whey proteins resist precipitation of protein molecules. (i) Under the condition where the environmental pH is equal to the isoelectric point of whey protein (ii) Under the condition where rennet is added to whey protein solution
You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])
What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9. Please show your answer as a percent of deprotonated N-terminal species relative to all (protonated and deprotonated) N-terminal species. Can you show your calculations so I can understand your method of approach?
Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.

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