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: Devise a laboratory exercise based on the Ehlrich test for Proteins 1. write a 3 paragraph…
A: Ehlrich test A biochemical test called the Ehrlich Test is used to find the amino acid tryptophan…
Q: A peptide has the sequence…
A: Solution - According to the question - Given - If pH > pKa, ionizing groups lose their protons.…
Q: viii) You have the following stock solutions available: 2.5M Tris, 0.5M Glycine and 10% SDS, how…
A: To prepare 1 liter solution of 25mM tris, 190mM glycine and 0.1% SDS can be prepared by following.
Q: what is the concentration of the unknown protein in nanometers? use the information below! protein…
A:
Q: 5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and…
A: Given , molecular weight of (no beta -Me ) purified sample = 97.4 kDa molecular weight of (beta -Me)…
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 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: which has the strongest IMF at coom termperatare? 0.) Brall) b.) la6s) C.)Falql
A: All the given species are non polar. In such species strength of intermolecular forces of attraction…
Q: The amino acid histidine has ionizable groups with pKa values of 1.8, 6.0, and 9.2, COOH H₂N-CH CH…
A: GIVEN The pKa1, pKa2 and pKa3 values of Histidine are given as 1.8, 6.0 and 9.2. Initial pH of…
Q: What trend can you suggest for the stability of proteins under varying pH
A: As we decrease the pH (by adding acid ) converts COO- ion to a neutral COOH group. In each case the…
Q: Calculate the number of millimoles(mmol)in 500 mg of each of the following amino acids: alanine…
A: The relation between mass, molar mass and mole is given by : Mole = mass/molar mass
Q: Which side chain would most likely be found in the interior of a protein, away from the aqueous…
A: Hydrophobic amino acids have little or no polarity in their side chains. The lack of polarity means…
Q: Protein synthesis in bacterial cells almost always starts with: a cysteine residue O could start…
A:
Q: Draw the structure for the peptide CF. • You do not have to consider stereochemistry. • You do not…
A: Given peptide, CF C- Cysteine F - Phenylalanine
Q: Trp b. Phe c. Tyr d. Pro
A: Trp is a symbol for Tryptophan amino acid. Phe is a symbol for Phenylalanine amino acid. Tyr is a…
Q: (b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0.…
A: Polypeptides are polymers of amino acids that make up proteins. The amino (–NH2) and carboxylic acid…
Q: In Hb S, a residue is replaced by a residue. histidine lysine valine
A: given, in Hb S, a ___ residue is replaced by a __ residue.
Q: Which representation of the amino acid lysine would exist at a pH less than the isoelectric point?…
A: Given amino acid,
Q: The isoelectric point (pl) of a peptide is the pH at which the Group pK peptide ceases to migrate in…
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: Which of the following peptides will elute last from a hydrophobic interaction column? A)…
A: From the given peptides we have to determine the peptide that is eluted last using hydrophobic…
Q: Two phenylalanine residues are separated by 1.0 nm in a polypeptide. Calculate the dispersion…
A: Dispersion force is the force of attraction that exist between atoms or molecules that developed…
Q: Reset Help The lipid bilayer consists of hydrophobic rows of with the forming the center of the…
A: We have given that The lipid bilayer consists of rows of With the…
Q: Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to…
A: A substance is said to be basic, if it has the ability to donate lone pairs.
Q: What is the major force responsible for the formation of an a-helix in protein secondary structure?…
A: In this question, we will see which force is responsible for making alpha helix in secondary…
Q: (a) Describe in detail how you will determine the primary structure of protein. (b)You have been…
A: The primary structure of a protein is generally referred to the sequence of amino acids in the…
Q: A protein is a large polypeptide. Polypeptides are polymers of amino acids joined together through a…
A: Concept: polypeptide bond is nothing but the amide linkage.
Q: protein has a number of aspartyl and gluatmyl residues, what would be the expected pI for this…
A: Answer The protein has number of aspartyl and glutamic…
Q: Make 2 amino acids models and capture them. Write down their names and if their model is
A: The question is based on the concept of biomolecules. amino acid is a type of biomolecules. we have…
Q: What is the name of this oligopeptide? Use the three letter and one letter nomenclature of the amino…
A: Two amino acids are linked to each other through a peptide bond [C(=O)-NH-]. Hence "n" number of…
Q: Mark the TRUE alternative for the following peptide: a) For a pH of 7.0 this peptide will migrate…
A: For an ionizable group on a peptide, if pH < pKa, the group remains protonated, and if pH >…
Q: Which of the following protein assays does not make use of the copper (I or II) ions in the…
A: The purpose of the protein assay is to determine the concentration of a protein out of different…
Q: Why are Guanidins and Amidins such strong bases?
A:
Q: The force constant katr of a backbone Ca – -C bond in a peptide is 250.0 kcal/mol/Angstrom² and the…
A: Given: Force constant (kstr) of bond = 250 Kcal/mol/Angstrom2 Equilibrium bond distance (r0) = 1.49…
Q: b. Draw phi-psi angles about a valine from a short peptide indicating: 1) a phi-angle of+100° and 2)…
A: The phi-angle is referred as the dihedral angle between the groups attached to the nitrogen of the…
Q: Given the chart of pKa’s below, calculate the isoelectric point for tyrosine
A: Isoelectric point (pI):The isoelectric point is the pH of an aqueous solution of an amino acid (or…
Q: The pKa values for the amino and carboxyl groups of alanine are 9.69 and 2.35, respectively.…
A: In any buffer, if any strong acid gets added then the existing conjugate salt basically abstracts…
Q: What does high NaCl do to protein that is bound to a Sp column?
A: Column chromatography: Column chromatography is used to separate charge analytes. Column…
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: Consider the following five weak acids: Succinic acid: pKa = 4.16HOBr: Ka = 2.06 x…
A: Given weak acids Succinic acid: pKa = 4.16HOBr: Ka = 2.06 x 10-9Dinicotinic: pKa =…
Q: A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of…
A:
Q: (a) Describe in detail how you will determine the primary structure of protein. You have been given…
A: (a) Primary structure of protein The primary structure of a protein is generally referred to the…
Q: The pK1, pK2, and pKR for the amino acid cysteine are 1.9, 10.7, and 8.4, respectively. At pH 5.0,…
A:
Q: The pKa for the side chain amino group in lysine is 10.4. If we were working at physiological pH…
A: At pH below the pKa for the amino acid is protonated and at pH above the pKa then it is…
Q: how could the formulation scientist prevent aggregation of a protein drug?
A: Protein aggregation: A biological phenomenon in which intrinsically misfolded proteins or disordered…
Q: The term used to separate a mixture of enantiomers of amino acids using chiral reagents? A)…
A: When enantiomer of mixture are separated using chiral reagent is called isomeric resolution . In…
Q: Modify isoleucine to show its structure at pH 1 and pH 13. Modify each amino acid by adding or…
A: Given : We have to predict the structure of given amino acid at different pH.
Q: For which of the following is the hydrophobic effect the main explanation. A) micelle formation by…
A: Hydrophobic effect can be defined as the tendency of non -polar substances to be in a fear of…
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- Reversed phase HPLC refers to the condition of stationary phase and a mobile phase of separation. Select the best condition A. A hydrophilic stationary phase is combined with a non-polar mobile phase. B. A hydrophilic stationary phase is combined with a polar mobile phase C. A hydrophobic stationary phase is combined with a polar mobile phase. D. A hydrophobic stationary phase is combined with a non-polar mobile phase. describe the statementQuestion 9: Please answer everything correctly and clearly! Thanks. Like will be given.1. Fill In the blank with the correct terms. a. Term for elemental cations that act as enzymatic cofactors. Tem for small organic molecules that act as enzymatic cofactors b. C. Part of the enzyme were chemical reactions occur. An enzyme that has multiple sites, some for reactions and others for reaction feedback control. Enzymes that are rather aggressive, and turned "off" by a protein segment untl they are activated. N a earch hp d. ai
- [5] please help me answer this question and show explanation/solution.In order to determine soluble sugars in date sample, the sugar should be extracted with a. 80% acetone b. acidified water O c. 80% ether d. 80% ethanol14. What factor determines which layer will be on the bottom of a separatory funnel? a. polarity b. density c. boiling point d. conductivity e. dielectric constant Your answer:
- Please help me how to answer d-f. Please show step by step for a better understanding. Thank you very much.d. 1) LDA OCH3 2) CH3CH2I е. 1) LDA 2) CH3I. Reversed phase HPLC refers to the condition of stationary phase and a mobile phase of separation. Select the best condition to describe the statement A. A hydrophilic stationary phase is combined with a non-polar mobile phase. B. A hydrophilic stationary phase is combined with a polar mobile phase C. A hydrophobic stationary phase is combined with a polar mobile phase. D. A hydrophobic stationary phase is combined with a non-polar mobile phase. . Select the true statement(s) of the refractive index detector in HPLC? A. It is more sensitive than a UV detector B. It does not respond to many solutes C. It can only be used for isocratic elution D. All above is true
- . Identify the following antioxidant molecule. A. alpha tocopherol hydroquinone dehydroascorbic acid CH3 CH3 C. alpha tocopherol semi-quinone \ / D. ascorbic acid C = C E. alpha tocopherol quinone / \ : O – C C – O CH3 \\ // \ / C – C C – CH2–CH2–CH2–CH–CH2–CH2–CH2–CH–CH2–CH2–CH2–CH–CH3 / \ / l l l CH3 CH2– CH2 CH3 CH3 CH3Please help answer D only... thanks!Please answer the last 3 sub-parts (#20-22)
