QUESTION 6If the 3 proteins in the blue sample had MW's of [1] 87,000 Daltons, [2] 30,000 Daltons, [3] 15,000Daltons; what is the MW of the protein in the 2nd band (counting from the origin) of the green sample?O O O Oa. about 15,000 daltonsb. about 87,000 daltonsc. more than 30,000 daltons but less than 87,000 daltonsd. about 30,000 daltonsCellular and Molecular Biology (6657

Gel electrophoresis is a technique used in molecular biology to separate biomolecules such as DNA,…

If the 3 proteins in the blue sample had MW's of [1] 87,000 Daltons, [2] 30,000 Daltons, [3] 15,000 Daltons; what is the MW of the protein in the 2nd band (counting from the origin) of the green sample? a. about 15,000 daltons b. about 87,000 daltons c. more than 30,000 daltons but less than 87,000 daltons d. about 30,000 daltons Cellular and Molecular Biology (665)

If the 3 proteins in the blue sample had MW's of [1] 87,000 Daltons, [2] 30,000 Daltons, [3] 15,000 Daltons; what is the MW of the protein in the 2nd band (counting from the origin) of the green sample? a. about 15,000 daltons b. about 87,000 daltons c. more than 30,000 daltons but less than 87,000 daltons d. about 30,000 daltons Cellular and Molecular Biology (665)

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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Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
Beta-sheets are roughly planar structures, in which the backbone hydrogen bonding pattern defines the plane. Where are the side chains in a sheet? Select one: a. The side-chains are on the outside of the sheet. O b. The side-chains are in the plane of the sheet, with residues from one chain on one side of the sheet, and residues from the other chain being on the other side. The side-chains do not have a consistent pattern. d. The side-chains are perpendicular to the plane of the sheet, with residues from one chain being above and residues from the other being below the plane of the sheet. C. e. The side-chains are perpendicular to the plane of the sheet, with residues from each chain alternating between above and below the plane of the sheet. O f. The side-chains are in the plane of the sheet, with residues from each chain alternating being on one side or the other of the sheet. g. Beta-sheets are rarely observed in proteins.
The limit for G-200 beads is 5000-600,000. When you pass two proteins- Protein A (75, 000), Protein B (1,000,000), through these beads, the protein that will elute out last is – They both elute out at the same time. Protein B Protein A
33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
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What can we most-accurately say about the polypeptide with the primary sequence KNEADING? a.It has two acidic R groups b.It has three basic R groups c. It has two nonpolar neutral R groups d. It contains three polar neutral R groups e. It contains a disulfide linkage
10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?