Leni, Isko and Ping are trying to determine the molecular weight of theircrude protein samples using SDS-PAGE. After running their samples, theyobtained the following bands in their gel.LadderLeniIskoPing1200 DaA1000 Da900 DaC800 Da700 DaF600 Da500 Da400 Da300 Da200 Da100 DaHDye fronta) Which protein/s is/are present in Leni's sample but not present in Isko andPing's sample?b) Which protein/s is/are present in Isko's sample but not present in Leni andPing's sample?c) Using the regression line, calculate the molecular weight of each proteinsubunits (A-H).|-|-|-001234.6.10

SDS-PAGE (sodium dodecyl sulphate–polyacrylamide gel electrophoresis), is a discontinuous…

Answered: Leni, Isko and Ping are trying to…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Label at least 10 bones on at least 3 different views from the pelvis and lower limb. You may choose any 10 bones.
A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein? (if applies, choose more than one) The protein consist of two 200kD subiunits The protein has a quaternary structure The protein is madeup of two 100 kD subunits Proteins is a tetramer consisting of 200 kD domains. The protein contains an impurity of 100kD
The data in the table are used to create a calibration curve for the determination of RNA from ts absorbance at 260 nm. Use a spreadsheet and the least-squares method to determine the slope and y-intercept of the best straight line fit to the calibration curve. Do not subtract the blank reading when creating the calibration curve. m= b = RNA (µg) 0.00 10.36 20.72 31.08 41.44 Absorbance at 260 nm 0.268 0.497 0.795 1.131 1.373 µg Using the slope and intercept of the calibration curve, determine the quantity of RNA in a sample that gives an absorbance of 0.699. -1
Using mass spec, the primary structure of 4 peptides is obtained from a tissue sample: VMDEL, GHKRT, CNPQI, and SAWFY. The pI of each peptide is calculated and ion exchange chromatography is used to purify each peptide. VMDEL, GHKRT, CNPQI, and SAWFY were separated into 4 pure samples. The labels on all the samples are erased by mistake, and the mass spec is no longer working. You can run a few simple tests to identify the samples. What are 4 tests to identify each peptide and why?
Look at the amino acid composition of a protein given in the table and click on the area in the 2D gel electrophoresis where you may expect the corresponding band. Amino acid composition M N P 7 3 11 A D E F G K R S V W Y ТОTAL: 16 2 12 14 4 1 3 7 2 11 11 10 1 164 Download Image. pH7 pH 9 pH3 200,000 116,250 97,400 66,200 45,000 31,000 21,500 14,400 ||| | |||
The following peptides were separated using ion-exchange chromatography based on the use of an anion exchange resin. Which peptide was eluted first? A B Peptide Name A B C D Molecular Weight (g/mol) 360 1080 1800 1440 Peptide Net Charge -2 -1 0 +1
A protein was purified to homogeneity. Determination of the mass by gel filtration chromatography yields 60 kd. Chromatography in the presence of the denaturing agent, 6 M urea, yields a 30 kd species. When the chromatography is repeated in the presence of 6 M urea and DTT, a single molecular species of 15 kd results. Describe what these experiments tell you about the structure of the proteins.
2q Which of the peptide sequences below best matches the hydropathy plot shown? 5 10 Residue Number RAFLILFMTYFLILFLI ILYYAGSREDHSGYLIL LHGDQNRERDGHSQERD EQSDTERNQHGALIYLI 3q Which of the peptide sequences below best matches the hydropathy plot shown? 5 10 Residue Number Hydropathy value -4 -2 0 2 4 Hydropathy value -4 -2 ILYYAGSREDHSGYLIL EQSDTERNQHGALIYLI LIFLAIFPAGSTSEDRR RAFLILFMTYFLILFLI L 15 15
Size exclusion chromatography is a protein purification method based on size. Larger proteins exit the column first, and smaller proteins exit the column last. Group of answer choices The SECOND statement is TRUE. The FIRST statement is TRUE. BOTH statements are TRUE. NONE of the statements are TRUE.
The data in the table are used to create a calibration curve for the determination of RNA from ts absorbance at 260 nm. Use a spreadsheet and the least-squares method to determine the slope and y-intercept of the best straight line fit to the calibration curve. Do not subtract the blank reading when creating the calibration curve. m = b = RNA (µg) 0.00 10.36 20.72 31.08 41.44 Absorbance at 260 nm 0.268 0.497 0.795 1.131 1.373 Hig Using the slope and intercept of the calibration curve, determine the quantity of RNA in a sample that gives an absorbance of 0.699.
Can you help me understand how to measure both protein A and B please
You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached. a. What type of protein-protein interaction do these results suggest? b. What amino acids are most likely involved in this interaction? (Guess based on assay)

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