Which of the following amino acid cannot bind a heme group using its side chain as an axial ligand? A. Lysine B. Valine C. Histidine D. Cystine

Q: ОН S. NH2 HO NH2 Thyrosine (tyr) Methionine (met)

A: Zwitter ion- it is as ion possessing both positive and negative electrical charges.

Q: a) This compound is an active HIV protease inhibitor b) This compound is an inactive HIV protease…

A: A virus that infects humans and mainly makes their immune system weak is known as the human…

Q: Explain if Biurent reagent reacts with free amino acids to form a colored complex

A: Given: To identify whether Biuret reagent reacts with free amino acids to form a colored complex.

Q: You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino…

A: The mixture of amino can be separated by electrophoresis technique. This method is based on pH…

Q: The manganese ion in the center is attached to aspartate ligand, 1 cysteine ligand, and 2 istidine…

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Q: “Chemisorption is highly specific.” Illustrate with an example.

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Q: What is the amino terminal residue? What is the carboxyl terminal residue? How many amino acid…

A: as per the policy guidelines we are here to solve first three questions only. amino acids are the…

Q: 40.) A protein with quaternary structure described as aBy would be a C) homodimer A) heterotrimer B)…

A: A protein with quaternary structure with alpha-beta gama has to be given,

Q: what is the relationskip between 36 1) Enomtiomevs 2) Draslueomers 3) Identical 4) Gpimev s

A: There are the concept of stereoisomers.

Q: What amino acid substitution would be accompanied by the largest decrease in enteric water penalty?…

A: Amino acid along with ionizing sie chain ,such as asp, glu, His, liz, impart important properties to…

Q: A peptide has the sequence…

A: Solution - According to the question - Given - If pH > pKa, ionizing groups lose their protons.…

Q: The initial pH of a 2M arginine solution is 14. What is the predominant structure of arginine in…

A: At pH = 14 , arginine exists in completely deprotonated form .

Q: The structure of haemoglobin: A. has an alpha-beta architecture. B. is a hetero tetramer. C. is a…

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Q: The maximum number of amino acid side chains that can potentially form an ionic bond (+lil-…

A: Histidine is an amino acid with a imidazole ring attached as a substituent. The polarity of…

Q: 29. The pH maximum for the reaction of primary amine and an aldehyde to form an imine is: а. 2 b.…

A: 29) The pH maximum for the reaction of primary amine and an aldehyde to form an imine is 4.5.

Q: The amino acid His is triprotic with pK1 (α-COOH) = 1.82, pK2 (α-NH3+) = 9.17, and pK3 (side chain)…

A: If the pKa of acid is equal or lower than the pH of the solution then the acid will get deprotonated…

Q: A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that…

A: In the amino acid has the two acidic hydrogens will be present. The first most acidic hydrogen is…

Q: An enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in…

A: Any enzyme can be categorised a certain protein which loses its activity at a certain temperature,…

Q: Explain how EDTA binds to a heavy metal

A: Interpretation: We have to tell how EDTA binds with heavy metal.

Q: Protein synthesis in bacterial cells almost always starts with: a cysteine residue O could start…

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Q: In the experiments of Barrick et al. (as shown), it was observed thatreplacement of histidine by a…

A: Hemoglobins have two alpha chains and two beta chains. When oxygen binds hemoglobin, there is a…

Q: Arginine and lysine side chains fit into trypsin’s binding pocket . One of these side chains forms a…

A:

Q: s Fe3+ is both enviromentally friendly is L UDdent in nature A in

A: The symbol Fe3+ represents iron in +3 oxidation state. It is also denoted as ferric ion. It is an…

Q: biochemical importance of plasma proteins? (e.g: globulin, abumuin, Fibrinogen)

A: Plasma protein also knows as blood protein serves many important functions:

Q: An antibody X binds to an antigen Y. When the antigen concentration is 3.0 x 10 M, 0 is 0.50. What…

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Q: A. Draw the structure of L-valine in a strongly basic solution. B. What is the charge of this amino…

A: “Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: 10. Draw the full chemical structure of the tetrapeptide G-H-F-A as it would look at pH 12.0. Use…

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Q: When Coomassie Brilliant Blue G-250 binds to the protein in solution, a shift in wavelength from 465…

A:

Q: You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino…

A: Electrophoresis- Separation of charged particles with the help of electric field. It consists of…

Q: Arginine has ionizable groups with pKa values of 2.17, 9.04, and 12.48. A researcher makes up 73 mL…

A: From the pKa values of arginine, it can be stated that, at pH 8.5 second proton is partially…

Q: 2+ The amino acid "arginine (Arg)" has the following form: Arg, HArg, H₂ Arg+, H3 Arg²+. Which is…

A: pH < pka (protonation) pH > pka (deprotonation) pH = 1/2 protonaton or deprotonation

Q: The amino acid (S)-alanine has the physical characteristics listed under the structure. How does the…

A: Enatiomers: Enatiomers can be defined by   saying that the optical active compounds which can rotate…

Q: 4) What is the K, for disodium asparaginate? asparagine: FM 132.119 TZ 2.00

A: Given: To determine: kb for disodium asparaginate.

Q: The amino acid sequence shown below is a short excerpt (residues 130-172) from the rod domain of an…

A: Following the rules of conservative amino acids, the amino acids that when replaced with a…

Q: Drag and drop the correct terms in front of their definitions (not all terms are used). 1. the…

A: Answer

Q: A plot of activity versus pH for an enzyme that functions in the cytosol of a cell at pH of about 7…

A: The activity of enzymes varies at different pH levels.

Q: 81. Indicate beloging to glycofrangulin. I. aglycone part is frangulin II. it is aglycone III.…

A:

Q: Some Protein P binds to 1 molecule of X. The fractional binding curve (θ vs. [Ligand]) shows that θ…

A: For binding of ligand to a protein, the fractional saturation (θ) is calculated using Hill equation:…

Q: peptide has the sequence

A: peptide sequence is:…

Q: 31. ________________ binds to and provides feedback inhibition for ATCase.

A: 31. ____CTP_____ binds to and provides feedback inhibition for ATCase.

Q: 29.) A protein with quaternary structure described as C2B2Y2 would be a C) homodimer A) homotrimer…

A: Proteins are the long chains of amino acids. Protein has different kind of structure like primary…

Q: AMINO pKa1 pKa2 ACID Proline 1.99 10.96 Tryptophan 2.38 9.39 Valine 2.32 9.62 Glutamine 2.17 9.13…

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Q: Suh and Savizky studied the thermodynamics of human a - lactalbumin (HLA) unfolding in the absence…

A: Thermodynamics is a field of physics that studies heat, function, and temperature in relation to…

Q: How can the Michaelis constant (Km) be identified and used to represent the affinity between the…

A: The correct answer is given below

Q: a. Tyrosine b. Alanine c. Leucine d. Asparagine 5. Draw a picture showing the details of the…

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Q: Which interaction(s) is/are involved in the primary structure of a protein (choose all that apply)?…

A: We know that primary structure of protein is the linear sequence of amino acids in a peptide or…

Q: . The _____________ plot shows the free energy change for a given amino acid window, allowing the…

A: Here we need a curve which shows the free energy change for a given amino acid window, allowing the…

Q: Almost all proteins are composed from a set of about _____ amino acids. a. 4 b. 10 c. 20 d. 50

A: Hello. Since you have posted multiple questions and not specified which question needs to be solved,…