Theoretically, the pI of myoglobin is 7.2. In phosphate buffer pH 6.0, what is the overall charge of myoglobin? How would it interact with CM Sepharose?

Compute for the albumin to globulin (A/G) ratio using these data given Albumin= 51.9g/L Total protein = 75.5 g/L Note: answer should be in ratio form

The protein calcineurin binds to the protein calmodulin with an association rate of 8.9 × 103 M−1 s −1 and an overall dissociation constant, Kd, of 10 nM. Calculate the dissociation rate, kd , including appropriate units.

80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL 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 relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.

Predict the diffusivity of human serum albumin at 293 K in water as a dilute solution and compare it with experimental data. Assume the following: The molecular weight of human serum albumin, MA= 72,300 kg/kmol The viscosity of water at 293 K is 0.897 x 10-3 Pa∙s The experimental data value is 5.93 x 10-11 m2/s.

Consider the following tripeptide:Gly—Ala—Vala. What is the approximate isoelectric point?b. In which direction will the tripeptide move if placed in anelectric field at pH 1, 5, 10, and 12?

Mixtures of amino acids can be analyzed by first separating the mixture into its components through ionexchange chromatography. Amino acids placed on a cation-exchange resin  containing sulfonate ( -SO3-) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) aggregation of nonpolar amino acid side chains with the hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Aspartate and lysine (b) Arginine and methionine(c) Glutamate and valine (d) Glycine and leucine (e) Serine and alanine

Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen Hemoglobin (monomer) 6.6 115 7.1 16 Myoglobin 7.0 16.7 From the given table, draw the appearance after visualization of a protein mixture containing the seven proteins in the table when subjected to SDS-PAGE.

Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…

A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)