1. Complete the table below with information about the amino acids utilized in this pro-cedure. Remember that smaller amino acids will travel further and so will amino acidsthat are soluble in the solvent.Table 9-1. Amino Acids ProcedureAMINO ACIDSPhenylalanineAspartic AcidLeucineProlinematempsDRAW THEMOLECULARSTRUCTUREinPOLARITY(IS ITPOLAR ORNONPOLAR?)odmeher basalu laMOLECULARWEIGHTSIZE (RANKLARGEST = 4ANDSMALLEST = 1)SHOULD ITREACT WITHNINHYDRIN?

Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

Answered: 1. Complete the table below with…

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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12 A Aa v AaBbCcDc AaBbCcDdEe AaBbCcDdE AaBbCcDdE Uv ab x, x A A v 三三三=|這、| 4、 Caption Emphasis Heading 1 Heading 3 Q2. Complete the table below with a tick to show which of the following statements describe the molecules. Statement Alpha glucose Fatty acid Amino Nucleotide acid A hexose sugar Insoluble in water Formed by condensation reactions Contain the elements, C, H and Contains the element, N Has a carboxyl group, -COOH Forms polypeptides >
ok-Personal Microsoft Edge com/maildeeplink 021 pdt Download Print Save to OneDrive 1. Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in aqueous solution at pH3D10.3. (Relevant pka values are: 2.2 4.3, 6.0, 9.8, and 10.1) Acp is adiusted to
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1. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 7? 2. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 12?
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=0
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
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Titration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.
I. Write a balanced chemical reaction, complete with chemical structures, to show the hydrolysis of iso-C to U. II. Draw the mechanism by which iso-G converts to its "minor tautomeric form complementary to U." You may propose either an acid or base catalyst. III. Draw chemical structures of the minor tautomeric form of iso-guanine (iso-G) and uracil (U), showing the non-covalent bonding (H-bonding) interactions between them.
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