which of the following about glycine- is true 9. Glycine is s an essentigl amine acid. b. Sylphyr eontaining at 4th pasition. guonidine group. opticolly Has a inactive.
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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.27. Draw palmitic acid, identify a, B and w carbons, write out its short hand notation 28. Examine the peptide sequence below and then answer the questions: H2N-Gly- Leu- Ala-Asp-Cys-Asn-Trp-lle-Ser-Phe-Lys-Cys-Arg-Pro-coOH a. Circle the asparagine residue b. A possible intramolecular disulfide bond can be formed within this peptide between which two residues? c. Circle one residue which has a positively charged side chain under pH 7.4 d. Circle one residue which has a negatively charged side chain under pH 7.4 e. Circle the residue which can be phosphorylatedRegarding to ALL the 20 standard amino acids1. Are ALL the 20 standard amino acids asymmetric and chiral molecules?2. Do they contain the elements C,H,N,O,S3. do they have high boiling oils at room temperature
- 29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.5710. o . Briefly discuss Ramchandran plot. . What is quaternary structure of proteins? Mention the role of various bond in its structure with the help of an example give its biochemical function. What are liposomes? Discuss their role in medicine. . Differentiate between cerebroside and ganglioside and one disorder associated with each. Rtyrosine 2. 3) Sketch the titration curve for apertic acid. Be sure to labeleach pk., the pl, zwitterion, and draw the dominant forms of the aminoacid along the curve just ke your lab report, the lecture slides and Figure 3.7 on page 69 of your textbook.
- 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…The ff. are neutral amino acids, except: ●A. methionine O B. lysine ● c. threonine O D. non of these 49s) 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).
- unu meleDy aln ncease In BIUUU giucose concentration. In the absence of glucose, cells rely on fats as a source of energy. 1. Protein Structure and Chemistry The primary structure of human insulin is shown below. It is made up of two polypeptide chains that come together in a quaternary structure. The first amino acid of each chain islabeled with the number 1. A handout with all amino acids and their structure and properties is provided on page 5. Primary structure of proteins 1a. Circle and label the amino and carboxyl ends in the primary structure of each polypeptide. Draw the appropriate functional groups at each end. Ceu Ala 1b. Identify and label one amino acid each with side groups that are: i) polar ii) non polar iii) acidic iv) basic Glu Chain B 30 amino acids His Secondary structure 1c. Show one H-bond that determines the secondary structure of the protein. You should indicate the bond in the diagram using appropriate functional groups. Gin Cya Chain A 21 amino acids Thr Gin…4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".8. The chemical structure of Coenzyme A contains the following except— a phosphoanhydride moiety. a β-mercaptoethylamine residue. a lipoic acid residue. a pantothenic acid residue. an adenosine-3’- phosphate.