Among these protein assays, which work in acidic conditions? a. Biuret assay b. Bicinchoninic acid assay c. Bradford assay d. Lowry assay

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…