A solution of peptide of unknown sequence was divided into 2 samples. One sample was treatedwith trypsin and the other one with pepsin. The fragments produced are given below:TRYPSINA. Pro-Gly-Met-Phe-Leu-ArgB. Gln-Ile-Pro-LysC. Ala-Gly-Trp-LysPEPSINA. Phe-Leu-Arg-Ala-GlyВ. Pro-Gly-MetС. Тrр-Lys-Gln-Пе-Pro-LysDeduce the original polypeptide chain.

Site specific proteases are enzymes that cleaves polypeptide chains only at specific sites i.e. at…

Answered: A solution of peptide of unknown…

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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Similar questions

Using an arrow, draw the site of cleavage for the following peptides that are reacted by: Pepsin (a- b), trypsin (c-d), and chymotrypsin (e).
1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
Draw the peptide at a pH @1 of Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?
Which of the following enzymes adds a new amino acid to the growing chain of a protein during protein synthesis? a. aminoacyl-tRNA synthetase b. peptidyl synthetase c. peptidyl transferase d. ribosomal synthetase
Consider this sequence below: GAG TAC ACG AGT GGA Which of the following options is an example of a non-synonymous point mutation? (remember to translate to mRNA!) A. GAG TAC AAT CGA GTG GA B. GAG TAC ACG GGT GGA C. GAG TAC A–G AGT GGA D. GAG TAC ACG AGA GGA
What is the effect of the altered amino acid sequence in Hb S that causes the cells to form sickle shapes?
1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)
A gene contains the sequence CGCATACGGTAC that results in the amino acid sequence arg-ile-arq- tyr. A mutation in this gene has a G inserted after the second C in the strand. How will this mutation affect the phenotype? A)This will affect the phenotype because although most of the protein will be identical, the first amino acid will be different. B)This will not affect the phenotype because only the second amino acid is different from the original protein. C)This will not affect the phenotype because the protein will be identical to the original protein. D)This will affect the phenotype because all of the amino acids after the first one will be different from the original protein.
Identify the correct matched protein related disorder * (Please choose one correct answer only) A. Kwashiorkor: prominent presence of edema due to protein and calorie deficiency B. Prion disease occurs due to the presence of tau proteins causing neurofibrillary tangles inside neurons C. Sickle cell anemia as an example of a point mutation replacing glutamic acid with valine and lysine in one of the beta chains of hemoglobin D. Ehlers-Danlos syndrome and Osteogenesis Imperfecta may share the same defects of on the type of fibril forming collagen of the gene
Why are structural analogs of sugar molecules (such as Oseltamivir and zanamivir) effective in treatment of influenza-virus infection?
Why is EF-Tu so important in E. coli?

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