The following protein crystal structure is the Human Serum Albumin complexed withoctadecanoic acid (PDB ID: 1E7I).According to the protein data bank, Human Serum Albumin is composed of 72% helical structure.Among the following options (a-c), select the possible Ramachandran plot for the above HumanSerum Albumin.(a)(b)(c)PhiPhiPhi Fill in the blank: Identify the type of non-covalent/covalent interactions present in the followingprotein tertiary structure at physiological condition. Be specific about the type of interactions. 1H.0-HOH OHCH,CH,H-CHCH,NH0-CH-OHCH.SISI

The Ramachandran plot also termed as Rama plot is the way to visualize the position of backbone…

Answered: Fill in the blank: Identify the type of…

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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Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
A sample (660 mg) of a (homo)oligomeric protein of molecular weight of 132,000 Da was treated with an excess of 2,4-dinitro-fluorobenzene until the reaction was complete. The peptide bonds were then completely hydrolyzed by heating with 6 M hydrochloric acid. The hydrolysate was found to contain 5.5 mg of the following compound. NO2 O2N- NH НООС 2,4-Dinitrophenyl derivatives of the amino groups of other amino acids were not found. a). How many polypeptide chains are there in this protein? Show your work. b). Assuming that each of the subunit contains entirely a-helices, how many a-helical turns would there be, approximately, in each of the subunit? "For a protein of typical composition, average amino acid residue mass is ca. 110 Da."
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.
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?
After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
The dissociation constant, Kd for a complex between protein A and protein B is 4.1 μM. If the two proteins are mixed together at initial concentrations of [A]= 0.025 μM and [B] = 4.7 μM, calculate (a) the equilibrium concentrations of A, B, and AB (the dimer formed by A and B) (b) the percentage of A bound to B
Histidine is an amino acid with three titratable groups: an -NH3+ group (pKa = 9.2), a -COOH group (pKa = 1.8), and an imidazole (amine-like) group (pKa = 6.0). The titration curve for histidine is shown below with four points highlighted. (a) Identify which point on the titration curve corresponds to the pKa for each of the titratable groups, and which point corresponds to the pI. Explain your choices. (b) Calculate the value of pI for histidine
When separated on a polyacrylamide gel, the procedure is abbreviated as SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). The technique is a standard means for separating proteins according to their molecular weight. The gels are neutral, hydrophilic, three-dimensional networks of long hydrocarbons cross-linked by methylene groups. (Give the main two compounds responsible for the formation of the gels)
The melanocyte-stimulating peptide hormone a-melanotropin has the following sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val (a) Write the sequence using the one-letter abbreviations. (b) Calculate the molecular weight of a-melanotropin, a da'
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species

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Fill in the blank: Identify the type of non-covalent/covalent interactions present in the following protein tertiary structure at physiological condition. Be specific about the type of interactions. 1 H-Q H. OH OH CH, CH, CH,