at punctures the bacterial cell wall has just been recently isolated from theF the peptide reveals the following information below: IOTE: when the sequence is nat knawn, a comma separates the amino acids)HydrazineAcid Hydrolysis (6 N HCI) at 110 °CHeptapeptide(2) Arg, Pro, Phe, Tyr, Ala, Lys2.4-dinitrofluorobenzeneDNP-PheLys andmodified freePeptide 1(Ala, Lys)amino acidsCleovoge with Trypsin, then chromatographyPeptide 2(Pro, Arg, Tyr)Peptide 3(Phe, Arg)PheCleavage with Chymotrypsin, then chromatographyPeptide 4(Arg, Tyr)Peptide 5(Lys, Pro, Ala, Arg)When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter.1. What is the C-terminal residue? K2. What is the N-terminal residue? F3. What is the sequence of Peptide 3? GP4. What is the sequence of Peptide 5? LPAA5. What is the averall amino acid sequence? AL

Trypsin cleave on the carboxy side of arginine and lysine residues. Chymotrypsin cleave on the…

Answered: at punctures the bacterial cell wall…

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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Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, Ion exchange chromatography is conducted via a software using DEAE-cellulose and method of elution is done by salt gradient. pH is set to 7. In terms of Molar, start of gradient is 0 and end of gradient is 1. The following graph is generated. Using the graph and analytical methods, determine pI of protein.
a protein pretreated with an sds page detergent shows two bands around 100 and 150 kD on the electrophoresis gel.Same protein is treated with the SDS and 2-mercaptoethanol reveal a single band 50 kd on gel.How many subunits would this protein contain
A certain plant storage protein, after being isolated, was digested using both 8N H2SO4 and conc. Ba(OH)2. The resulting hydrolysates were then analyzed for amino acid composition using paper chromatography with EtOH-NH3-H2O (80:10:10) as the solvent system and ninhydrin as the visualizing agent. Name the amino acids found in the acid hydrolysate labelled 1-5.
I. Buffer Preparation A researcher in Biochemistry is isolating α-glucosidase enzyme from malted wheat flour. The protocol requires the use of 2.00L of 0.225 M of lactate buffer with pH of 4.25. How will he/she prepare this buffer from 2.00 M lactic acid solution and solid sodium lactate (NaC3H5O3) The Ka of lactic acid is 1.38 x 10-4. [ Na=23.0, C=12.0, H=1.01, O=16.0 g/mol]
A researcher has synthesized two peptides and needs to confirm whether the peptides were synthesized with the correct sequence using mass spectrometry. What is the sequence of the b4 and y7 ions for peptide GAMECHANGER? The peptide SLISRAEFLAGVRVGV is digested with trypsin. Then the products of the digestion are subjected to ESI TOF-MS in positive ion mode with the peptides in a pH 2 solution. What peptide fragments will result and what are their m/z?
Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous solution at pH=10.3. (Relevant pKa values are: 2.2,4.3,6.0,9.8 and 10.1)
You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculations
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
The octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.
Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, size exclusion chromatography is being done. Use the graph below and analytical methods to determine molecular weight of protein.
200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.
The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groups

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