Please answer and explain this Biochemsitry Question to the best of your ability Protein Sequencing ProblemsTo get you started, here is a table with the specificities for some of the enzymaticand chemical procedures used in sequencing proteins:ProcedureEdman DegradationCarboxypeptidase ACarboxypeptidase BCyanogen BromideaminoethylationTrypsinChymotrypsinStaphylococccus aureus V8ProteaseAnhydrous Cyanogen Bromide C side of RSubmaxillarus ProteaseEndoproteinase Lys CAsp-N-proteaseThermolysinPepsinAcid PhosphataseAcid HydrolysisSiteR₁-1R₂C side of N terminus R = any amino acidN side of C terminus R, # Arg, Lys, ProR₁-1 ProN side of C terminus R Arg, Lys, AECysR₁-1 # ProR = MetC side of R₁Cys residueC side of RCside of RC side of RC side of R₁C side of RN side of RN side of R₁N side of RSpecificityC side of R₁Breaks all peptidebondsRn+1R = Met, TrpReacts with Cys to giveAECysR = Lys, Arg, AECysR₂+1 #ProR - Phe, Trp, Tyr, LeuR₁+1 #ProR = Asp D, Glu ER = ArgR = Lys KR = Asp D, Glu ECommentIneffective for blocked N terminiRemoves 1 (usually up to 4) residuessequentiallyRemoves 1 (usually up to 4) residuessequentiallyHighly SpecificHighly SpecificHighly SpecificSometimes cleaves at other sitesR = Leu, Ile, Phe, Trp, Tyr, Sometimes cleaves at other sitesValR₁+1 #ProR = Leu, Asp, Glu, Phe,Tyr, TrpR₁+1 # ProR = Asp, GluThe table uses terms like "R". I've drawn a short piece of polypeptide so youcan visualize where these cleavages are taking place.N side of R₁Fairly nonspecificHighly SpecificC side of R₁If the amino acids are listed with dashes connecting them, they are in sequence.If the amino acids are listed separated by commas, they are not in order.For example.....If I treat G-K-A-V-M with trypsin I will get two pieces. One will be (G-K) andthe other will be (A-V-M). If I only know the composition (and not the actualsequence for these pieces) it would be written (G, K) and (A, M, V). 1. Lets start by determining the products we would get from treating apolypeptide with some of the procedures above.Using the polypeptideA-R-D-K-P-C-F-M-P-N-GA) What would acid hydrolysis give you? What would you get if youused Chymotrypsin?B) What would you get if you used Cyanogen bromide?C) What would you get if you used Trypsin? How about using Trypsinafter aminoethylation?

A peptide is a short chain of amino acid residues linked together via peptide bonds. The peptide…

1. Lets start by determining the products we would get from treating a polypeptide with some of the procedures above. Using the polypeptide A-R-D-K-P-C-F-M-P-N-G A) What would acid hydrolysis give you? What would you get if you used Chymotrypsin? B) What would you get if you used Cyanogen bromide? C) What would you get if you used Trypsin? How about using Trypsin after aminoethylation?

1. Lets start by determining the products we would get from treating a polypeptide with some of the procedures above. Using the polypeptide A-R-D-K-P-C-F-M-P-N-G A) What would acid hydrolysis give you? What would you get if you used Chymotrypsin? B) What would you get if you used Cyanogen bromide? C) What would you get if you used Trypsin? How about using Trypsin after aminoethylation?

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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