ANSWER THE FOLLOWING PROBLEM AND EXPLAIN YOUR ANSWER FOR BETTER UNDERSTANDING. No. 3. Which Amino acids are zwitterionic? D se esse B 3 0 N Ol lov
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- Answer the questions regarding the tripeptide shown. H3N-CH- -C N-CH-C-N-CH-C-O | CH СНОН H CH2 H3C CH3 CH3 SH Which amino acid is the C-terminal amino acid? threonine cysteine methionine valine What is the name'of this tripeptide, using the three-letter amino acid abbreviations? Capitalize the first letDraw the Haworth projection and chair conformation for the following carbohydrates.Given the following peptide, answer following questions 1-5: CO CH2 O || CH2 O H3N-CH-C-NH- CH-c-OCH3 | 1. Is this a dipeptide or tripeptide? 2. How many amino acid components/residues are there? 3. Name these amino acids. 4. What kind of bond links these amino acids? 5. The above structure represents the major ingredient in some commercial product(s). Identify the name of this major ingredient or the commercial product(s). Given that the hemagglutininin protein in influenza virus contains a remarkably long a-helix with 53 residues, answer questions 6-7. 6. How long is this a-helix (in nm)? Show all calculations. 7. How many turns does this helix have? Show all calculations.
- Consider the following molecule. a. Name it.b. Use the three-letter symbols for the amino acids torepresent this molecule.A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________ Indicate whether each of the following statements describes a reversible competitive inhibitor, reversible noncompetitive inhibition, or an irreversible inhibitor. ________ a. It bonds covalently to the active site ________ b. The inhibitor effect can be reversed by the addition of more substrate ________ c. Inhibitor structure resembles that of the substrate ________ d. The inhibitor and substrate cannot bind to the enzyme simultaneously.A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________
- 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. inExamine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.Answer the following questions: a. How many possible stereoisomers does D-ribose have? b. What bond is present between the fatty acyl group and the C-2 amino group of sphingosine in a Ceramide?
- 1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…Write down the abbreviations (both 1 letter and 3 letter) for the amino acids given below:Tryptophan, Glutamine, Isoleucine, Cysteine, ArginineDraw the stereoisomers of the following amino acids. Indicate pairs of enantiomers and pairs of diastereomers. leucineCH3CHCH2 CHCOO−CH3 +NH3 isoleucineCH3CH2CH CHCOO−CH3