1. Sodium error encountered in using a pH meter causes a/an increase in the pH reading of a solution than the actual pH reading. 2. The pH of amino acid is adjusted to 1.5 prior to titration to make sure that the amino acid has a net positive charge. 3. Protein is most soluble in a solution with pH equal to its isoelectric point (IpH).
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- 1. List down the amino acids in the following format Amino Acid Physiological Significance 3 letter Code 1 letter code Chemical Structure 2. List down the different qualitative and quantitative tests for Amino Acids Test Reagents Principle Positive Reaction/ResultChoose among proteins A, B, C, and D. 1. Protein that will most strongly bind to an anion exchange colum. 2. Protein that will elute last in gel filtration chromatography. 3. Protein that will elute first in hydrophobic interaction chromatography. 4. Protein that will elute last in a carbohydrate containing colum.2. Vasopressin, a substance produced by the human body that regulates blood volume and pressure, is a nonapeptide with the following amino acid sequence. Describe the results you would expect when vasopressin is tested with the following reagents. sort GLY-ARG-PRO-CYS-ASN-GLN-PHE-TYR-CYS test xanthoproteic Millon's Hopkins-Cole nitroprusside observation A 250 25d ZYN CZ, ZINTEG DST ZW
- 1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?A protein has a sedimentation coefficient of 2.6S, when ultracentrifuged in a 0.1 M NaCl solution; the same protein has a sedimentation coefficient of 4.6S, when centrifuged in a 1.0 M NaCl solution. This change in the sedimentation rate at 1.0 M NaCl, most likely occurs because the protein. (one word = verb).You had a second solution with an unknown concentration of Protein X that had to be diluted 4x before you could measure the absorbance. The diluted solution had an absorbance of 0.76. What is the concentration of the diluted solution in ug/ml and what is the concentration of the original solution
- 1. How do you prepare 25 mL of a 0.4X solution of SDS from a 20X stock?2. How do you prepare 50 mL of a 0.25X solution of Trisethylenediaminetetraacetic acid (TE) buffer from a 100X stock?Which of the following will happen if perchloric acid is added to a neutral polysaccharide gel? (Select 2 Possible Answers) a. increases gel formation b. decreases gel formation c. increases sol formation d. decreases sol formationAre Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 2. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
- 4. What is the region/point where AA is predominantly present as a (-2)-charged species?5. The effective buffering range for the amino acid in the acidic region is?6. What is the region/point where the solution has a 50:50 percent mixture of the (0) and the (-1) species?What will happen if you treat your protein solution with each of these shown below. 1. sodium dodecyl sulfate (SDS) (two different things happen) 2. A Reducing agent 3. BenzeneWhen acids are added to a solution, the pH should ___________ . a. decrease b. increase c. stay the same d. cannot tell without testing