Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- 5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0arrow_forwardChoose A if the statement is CORRECT B if the statement is WRONG This amino acid is/has: polar charged basic side chain 6. 7. 8. 9. aromatic side chain 10. K H H H N-C-C CH₂ CH ₂ CH₂ CH ₂ -Z N I NH₂ =O OHarrow_forwardWhich of the amino acid side-chains would you expect to be protonated (i.e. has not lost its proton) under neutral pH conditions? Include reasons supporting your prediction.arrow_forward
- Consider this structure. NH₂ N N O P O N N Part 1 of 3 HO Identify the monosaccharide. Select the single best answer. D-ribose D-2-deoxyribose Part: 1/3 Part 2 of 3 Identify the base. Select the single best answer. Othymine O guanine ○ cytosine adenine uracilarrow_forwardCan you please explain how to solve this problem?arrow_forwardIdentify what type of chemical interactions is involved in the following side chains of the peptide chain below: 3 H-Q 0-H 5. OH OH CH, 6. 9. 4. -- CH, 2. 200 CH, 12 CH CH, -NH,0-C 4 1. 15 3. CH.-OH O CH. 17 18 The following choices can be applied for the following type of chemical interactions. 20 21 Write: AB - if it is a salt bridge or ionic bond CD - if it's a H-bonding 23 24 EF - if it's a hydrophobic interactions GH - if it's a disulfide bondarrow_forward
- Would each of the following ions of serine exist at a pH above, below, or at its pI? Drag the appropriate items to their respective bins. Above pl H₂N-CH-COO CH₂OH H₂N-CH-COOH CH₂OH Below pl H₂N-CH-COO CH₂OH At its pl Reset Helparrow_forward2) Consider the following disaccharide which was formed from the breakdown of a polysaccharide found in plant material. ОН Glycosidic linkage: H H OH H H НО H H. OH H. ОН OH H НО H ОН a. Label the glycosidic linkage above in the following format: a/B(# → #) b. Would you expect this disaccharide to have been formed from amylose or amylopectin? c. Describe at least two chemical tests that would give insight into the structure of this disaccharide, assuming you've isolated it and wanted to elucidate the structure from scratch. Include detail on not only the tests you would use but what results you would expect to get given the structure above. Assume you can analyze the structure of any monosaccharide you get from your chemical tests.arrow_forward6arrow_forward
- The structure given is NH OH 'N' HO-P=0 ÓH A uridine monophosphate deoxycytidylate C thymidylic acid uridylatearrow_forward4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pIarrow_forward13. The structures of sphingosine and choline are given below. Draw the condensed structure and block diagram of the sphingolipid formed from these molecules and a molecule of myristic acid. CH3-(CH2)12-CH=CH-CH-OH CH₂ CH3-N-CH2-CH2-OH CH-NH2 sphingosine CH2-OH CH3 choline BLOCK DIAGRAM (draw below) CONDENSED STRUCTURE 14. Which fatty acid below should have the highest melting point? Why? Explain your answer based on structure and forces of attraction. OH O OH TOH OHarrow_forward
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