The following list of proteins are found in a mixture and are to be separated by 2D gel electrophoresis: Isoelectric point Protein Myoglobin Cytochrome C Molecular weight (Daltons) 17,000 7.0 10.6 12,000 150,000 IgG 6.4 Hemoglobin 64,500 5,800 66,000 15,000 33,000 7.1 Insulin 5.4 Human serum albumin 4.6 Histone H3 10.8 Pepsin 1.0 In 2D electrophoresis, the mixture is first subjected to isoelectric focusing, separating them via their isoelectric pH values (corresponding to the horizontal axis, then subjected to SDS-PAGE to separate via molecular weight (corresponding to the vertical axis), where large proteins stay at top and smaller proteins go towards the bottom. 4 pH 7 10 direction of electric current 150 MW (KDa) 100 в E A F. G 2 pH 7 10 With this information, match the letters of the bands to the proper protein based on the data given. Band Letter Protein

The following list of proteins are found in a mixture and are to be separated by 2D gel electrophoresis: Isoelectric point Protein Myoglobin Cytochrome C Molecular weight (Daltons) 17,000 7.0 10.6 12,000 150,000 IgG 6.4 Hemoglobin 64,500 5,800 66,000 15,000 33,000 7.1 Insulin 5.4 Human serum albumin 4.6 Histone H3 10.8 Pepsin 1.0 In 2D electrophoresis, the mixture is first subjected to isoelectric focusing, separating them via their isoelectric pH values (corresponding to the horizontal axis, then subjected to SDS-PAGE to separate via molecular weight (corresponding to the vertical axis), where large proteins stay at top and smaller proteins go towards the bottom. 4 pH 7 10 direction of electric current 150 MW (KDa) 100 в E A F. G 2 pH 7 10 With this information, match the letters of the bands to the proper protein based on the data given. Band Letter Protein

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

"Loops of polypeptide that protrude from the surface of a protein often form the binding sites for other molecules" is true or false.
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
What is the FIBROUS PROTEIN as the classification of proteins based on shape or conformation? Please do not plagiarize from the internet and provide your references.
Gelatin is a protein-water combination that is mostly water.Justify the formation of a solid from a water-protein combination.
Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..
Study the following data and its description. Write a conclusion of what you observe for each of the proteins tested in the experiment which are 4 in total
Which of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gel
What features of protein structure allow separation by Size exclusion ("gel-filtration") chromatography: (explain your answer)
Given this: 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 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly using SDS page?