In a mixture of the five proteins listed below, which should elute second in size- exclusion (gel- filtration) chromatography? A) cytochrome c B) ribonuclease A C) immunoglobulin G D) RNA polymerase E) M, = 13,000 Da M. = 13,700 Da M. = 145,000 Da M. = 450,000 Da M. = 68,500 Da %3D %3! %3D serum albumin %3D

In a mixture of the five proteins listed below, which should elute second in size- exclusion (gel- filtration) chromatography? A) cytochrome c B) ribonuclease A C) immunoglobulin G D) RNA polymerase E) M, = 13,000 Da M. = 13,700 Da M. = 145,000 Da M. = 450,000 Da M. = 68,500 Da %3D %3! %3D serum albumin %3D

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy). When you ran this protein directly on reversed phase-HPLC with UV monitor set at 280 nm, two peaks were resolved. Mass spec determined that the peaks represented Chain A and Chain B, respectively. The peak area is 500,000 for Peak A (Chain A) and 100,000 for Peak B (Chain B). The molecular masses of Chain A and Chain B are 25,000 and 5000, respectively. The extinction coefficients for Chain A and Chain B are 1 mL/mg.cm and 0.5 mL/mg.cm, respectively. Please calculate x/y.
About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.
+Protein Mr pl А 12,000 28,000 42,000 66,000 (a;) 103,000 (a2) 111,000 3 8.4 C 7.2 9 E 5 F 4.2 Predict how the proteins listed above will behave in a variety of separation and characterization procedures. For each chromatographic technique (you may assume that the protein remains “native," or non-denatured), list the order in which the proteins will elute (come of the end of the column): Size Exclusion Chromatography, pH 6.8 First Last Anion Exchange Chromatography, pH 9, using a salt gradient to elute First Last
Of the following methods listed below, which could not be used to obtain a reasonable estimate of the molecular mass of a monomeric protein? Select all that apply. O Electrospray ionization mass spectrometrylsoelectric focusing O Gel filtration O All of these methods could be used O Isoelectric focusing O Sodium dodecyl sulfate polyacrylamide gel electrophoresis O Total amino acid sequence determination by Edman degradation
What are two ways to measure the total amount of all proteins in a purification sample? O 1) Calculating the yield and 2) calculating the purity of a purification. O 1) Measuring absorbance at 280 nm and 2) using an enzymatic assay for your protein of interest. O 1) Quantitating the amount of your protein of interest using binding of a labeled antibody (e.g.. an ELISA) and 2) using a dye-binding assay. O 1) Measuring absorbance at 280 nm and 2) using a dye-binding assay.
The negative ion mode electrospray ionization (ESI) mass spectrum of an oligonucleotide shows peaks at the following m/z ratios: 2903.8 (40%), 2580.9 (67%) , 2323.7 ( 100 % ) , 2111.4 (71%), and 1935.7 (38%). What is the molecular weight of this molecule? Please show your calculations and use all peaks to determine significant figures.
Biuret Assay accurately quantify protein concentration within the range of 5-150 mg/mL. JUSTIFY THE STATEMENT.
What are analytes and how can they be used for biochemical recognition?
Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true.pls explain
What kind of chromatography would you for purification of full length antibody ?
macollege.instructure.com/courses/352/pages/covid-proteins-lab-manual?module_item_id=D44333 A = abc Where "A" is absorbance, "a" is molar absorptivity, "b" is the path length (length of the cuvette in units of cm), and "c" is concentration (mol/L). The molar absorptivity is an intrinsic property of a molecule which tells us how intensely it will absorb at a particular wavelength. If "A" is a unitless quantity, "b" is in units of cm, and "c" is in units of mol/L, then what are the units of molar absorptivity? Do a little research to learn how alpha-helices and beta-sheets are drawn in protein structures. If most of the absorption properties are coming from the alpha-helices in these proteins, and many alpha-helices have similar absorbance properties across different proteins, which protein would you predict would have the highest molar absorptivity? Your job is to use the following data table to determine the molar absorptivity for each of the following proteins at their respective…
Chemistry how would you isolate the glycosylated insulin from the unglhcosylated forms? can you come up with a method to purify the protein (insulin with sugar group)? It can be a column or a combination of columns. (hint: use size exclusion chromatography or other method and affinity concept.)