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…

Answered: 1. Lets start by determining the…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter30: Protein Synthesis

Section: Chapter Questions

Problem 19P

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Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?
HELPFUL INFORMATION: When doing automated sequencing, on the other hand, all 4 dideoxynucleotides are added to the same sequencing reaction, and run together in a single capillary gel. 1b What's the difference why can an automated sequencing reaction be done with all 4 dideoxynucleotides mixed together and run together, but not a conventional sequencing reaction?
RECALL Which of the following statements is (are) true? (a) Bacterial ribosomes consist of 40S and 60S subunits. (b) Prokaryotic DNA is normally complexed with histones. (c) Prokaryotic DNA normally exists as a closed circle. (d) Circular DNA is supercoiled
Pls help ASAP, thank you! "An alpha-helical structure within a protein is stabilized mostly by"
Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG
Question based on SDS-PAGE You are working with a 60 kDa protein that you want to visualize on a SDS-PAGE. What % separating gel will you use in your SDS-PAGE?
GABA (B) protein Need help answering questions about the GABA(B) protein. What is the primary structure Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein)What is the tertiary structure (which should also show secondary structure)Does the protein have a quaternary structure, if so what is it?
the image is the steps for help. Not writing assignment!!!! What is the intended outcome of the lysozyme-based ion exchange chromatography described above? Will the protein be effectively separated using the materials listed in the image, or will it fail? Give a brief explanation for your decision.
Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…
Chymotrypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: C-1 G-A-E-A-T-E C-2 G-K-V-G-A-H-A-G-E-Y C-3 V-L-S-P-A-K-T-N-V-K-A-A-W What is the sequence for the peptide? NOTE: Label the fragments when reconstructing the peptide chain e.g. for trypsin T-1, T-2 etc...
Calculating human genome If 1.5 percent of the human genome consists of protein-coding sequences, and the entire genome has 3.2x10^9, how many codons are there in the human genome? Remember that a codon is three nucleotides in length.
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