how to read this table? like for example, just by looking at the table, it was said that leptin has 16 kda with 15% gel. How did they able to determine that leptin needs 15% gel?
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how to read this table? like for example, just by looking at the table, it was said that leptin has 16 kda with 15% gel. How did they able to determine that leptin needs 15% gel?
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- HOW MANY of the following five items represent modes of protein denaturation? 1.) heating a protein sample 2.) cooling a protein sample (slowly) 3.) putting a protein sample in a saltier environment 4.) eating a protein sample (such as with a whisk) 5.) adding acid to a protein sampleAfter processing all of your protein samples in the laboratory, you are left with one sample to complete. How are you going to resolve the problem safely?At high salt concentration, proteins are less soluble. Changing the solubility of a protein based on the concentration of a highly soluble salt is the basis of salt precipitation. Group of answer choices BOTH statements are TRUE. The SECOND statement is TRUE. NONE of the statements are TRUE. The FIRST statement is TRUE.
- Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073xThe elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatographyWhich of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.
- Which factors will cause protein denaturation? Group of answer choices a. aqueous phosphate buffer b. heavy metals - Hg2+, Pb2+, Ag+ c. small metal ions - Na+, Ca2+, Cl- d. changes in pH e. use of detergents or soaps f. Tris a buffer commonly used with proteinsWhich of the following is not one of the basic features used in protein separation techniques? a. Specific binding affinity of protein b. Protein charge c. Viscosity of the protein d. Solubility of proteinUsing ultrafiltration, you concentrate a solution of Protein X as follows: Initial volume protein X = 300 mL Initial concentration protein X = 12 mg/mL Final volume protein X = 15 mL What's the final concentration of protein X in mg/mL?
- match the letters of the bands to the proper protein based on the given dataDetermine the number of proteins composed of 100 Amino acid... The solution read: total proteins composed of 100 nucleotides is equal to 20100 The solution should read total proteins composed of 100 Amino acids is equal to 20100 I did have someone answer me earlier about how to obtain the solution, however, I just believe there is a typo is the solution text. We are not looking for nucleotides, we are looking for Amino acids. So it should read total proteins composed of 100 amino acids is equal to 20100. If we were looking for nucleotides it would read 4100You're on duty at a prominent Metro laboratory. You mixed up a sample for protein analysis of the samples needed for forensic examination that contains pure DNA while waiting for your closest friend. You decided to use the knowledge you gained in Biochemistry to run the combined samples through a spectrophotometer to eliminate contaminated protein. Determine which of the samples should be extracted and separated for protein analysis based on the following data. Show all of your solutions. A230 A260 A280 Buffer 0.051 0.091 0.065 Sample A 1.27 4.54 2.01 Sample B 1.32 3.92 2.11 Sample C 1.95 3.88 2.04 Sample D 1.44 4.21 2.32