Plus pole pH 11.0 Middle of Paper Minus pole Aspartate Lysine Leucine Histidine Example amino acic
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- 0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.COLOR TESTS FOR PROTEINS AND SPECIFIC AMINO ACIDS Explain why essential amino acids (EAA) are indispensable. Enumerate the EAAs. Give the structure and name of tetrapeptide, phe-asp-leu-lys.what is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.
- High salt concentrations tend to cause protein aggregation. Suggest a way to identify proteins normalexpressed in particular bacterial species that can retaintheir solubility despite high salt conditions.The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? ExplainDetermine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
- Identify the structure of the predominant form of the pentapeptide at pH = 12 if there is a pentapeptide Ile-Lys-Asp-Phe-GlyNAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12pQLSeysIVg8-5-v0riWm3uEQ4RUA3Hdua_NDMQI25SST619X-KVA/viewform What makes alanine a nonpolar, neutral amino acid? O The presence of a chiral carbon O The hydrocarbon group attached O The zwitterion cannot be formed due to nonpolarity O The acid and base groups neutralizes the side chains What is NOT true about hemoglobin? It is a fibrous protein that helps oxygen combine with carbon It has an iron atom inside the structure It contains four polypeptide units O It transports oxygen to the different cells in the body
- 7. 1 B e here to search Required Study the two diagrams below. Diagram A 2 1 Diagram B 2 Based on the sequence of steps (1, 2, 3), which of the diagrams shows what would happen to proteins made at the ribosomes and transported to the outside of the cell? Diagram A Diagram B Both Diagram A and Diagram B Neither Diagram A nor Diagram B DELL 40)s) This is a Fish er projecti on of D-f ructose (Fisher projecti on of L-F ructose ). Dra w L-fructose. Inaddition, draw the Haworth projection of a-D fructofuranose and b-D fructofuranose, the cyclic form ofthis monosaccharide. Draw sucrose where indicated below (Haworth projection).wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZ