7. Will denaturation change the primary sequence of the proteins? Why or why not?8. Why was distilled water included in the samples tested? InstructionsUpon performing the xanthoproteic acid test, sulfur test, biuret test, and ninhydrin test, andprotein denaturation methods on various samples, the tables show the results of the experiment.The student is required to answer the questions relating to the data presented.Table A.Xanthoproteic TestSulfur TestAlbuminSlightly Opaque, OrangeSlightly opaque, brownCaseinSlightly Opaque, OrangeTransparent, light brown tintGelatinTransparent, YellowTransparent, ColorlessGlycineColorlessDistilled WaterColorlessTransparent, ColorlessCysteineOpaque, Black with ppt.TyrosineTransparent, YellowTryptophanTransparent, Dark OrangeTable B.Biuret TestNinhydrinTestAlbuminTransparent, PurpleOpaque, Dark blueCaseinSlightly opaque, Pink-purpleOpaque, Dark blueGelatinTransparent, Blue-PurpleTransparent, BlueGlycineClear, Light blueOpaque, Dark blueDistilled WaterClear, Light blueTransparent, ColorlessAlbuminGelatinDistilled WaterHeller's TestHeat without HC2H3O2+Picric Acid+Ethanol+HgCl2+

Denaturation: a. Protein when exists in its native state is most stable and soluble. b. It has the…

Answered: Will denaturation change the primary…

Will denaturation change the primary sequence of the proteins? Why or why not? 8. Why was distilled water included in the samples tested?

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

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8. Provide the structure of guanine, a heterocyclic base found in DNA. 9. Provide the structure of adenosine, a nucleoside. 10. Provide the structure of cytidine 5’-monophosphate, a nucleotide consisting of a cytosine base, a ribose and a phosphate group.
1. For each of the sequences given below, list what type of secondary structural element, if any is most likely to be formed by that amino acid sequence. 1a. SEGEWQLVLHVWA 1b. GKGPPGPPGPRGPC 1c. CHSRHPGDFSC 1d. ASVRMNLGF
14. Draw the structure of a U•A•U base triple. Draw hydrogen bonds as dashed lines, and draw hydrogen atoms involved in hydrogen bonds. How many base pairs exist in this base triple? Indicate the position of the ribose with an "R" (you do not need to draw the ribose. Use separate page/back if necessary).
3. You isolate DNA from 1 ml of a suspension of E. coli cells using the procedure outlined in your lab handout. After completing the DNA isolation procedure, the total volume of the DNA solution is 600 ul. You transfer 10 µl of this DNA solution into 490 µl of TE buffer to create a diluted DNA solution. Using a spectrophotometer, you determine that the concentration of the diluted DNA solution is 245 ug/ml. a. How much did you dilute the original DNA solution? Express the dilution as a ratio. b. What is the concentration of the original DNA solution? c. How much total DNA did you isolate from the suspension of E. coli cells?
2. You are in a South American rain forest looking for naturally occuring peptides with potential as drugs. You have a mobile biochemistry lab with common reagents and enzymes, an amino-acid analyzer, gel- filtration and ion-exchange chromatography, and electrophoresis. You also have an Edman Sequenator, but you have contaminated one or more of your reagents, and as a result, you cannot sequence peptides longer than about 12 residues before contaminants obscure the results. While screening extracts from the ovaries of an tropical orchid, you find a peptide with potential as an antiviral. Deduce its amino-acid sequence using the available tools. a) MW by electrophoresis can tell you how big a sequencing problem you are up against. Result: about 4000 b) Amino-acid analysis can help you decide how to fragment the peptide for sequencing: Result: A₂C₂D₂E4FG3HKLMN₂P2Q2R4S4T3W c) How many peptides expected from each of these possible cleavage reagents? Cyanogen bromide (C-side of M). Staph.…
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How would a copper bowl effect the denaturation of the proteins when mixed?
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1. In the SDS-PAGE figure below, looking at lane 6 there are two bands MamP, monomer and MamP dimer (disulfide bonded). Why does the MamP monomer run faster on the gel relative to the MamP dimer? 1 2 3 4 5 6 250 - 130 - 100 70 55 - Hisg MBPtev.Mamf MamP dimer 35 - 25- - MamP monomer 15 - 10 - If the gel was run under non-reducing conditions, would the pattern possibly be different and why? Molecular weight (kD)