What amino acids will be positive at a pH of 2? Use the pKa table TABLE 5.1 Properties of the common amino acids found in proteinspK₂ of a-COOHGroupªNameAlanineArginineAsparagineAspartic acidCysteineGlutamineGlutamic acidGlycineHistidineIsoleucineLeucineLysineMethioninePhenylalanineProlineSerineThreonineTryptophanAbbreviations: 1-and 3-letter codesA, AlaR, ArgN, AsnD, AspC, CysQ, GinE, GluG, GlyH, HisI, lleL, LeuK, LysM, MetF, PheP, ProS, SerT, ThrW, TrpY, TyrV, Val2.32.22.02.11.82.22.22.31.82.42.42.22.31.82.02.22.62.42.22.3pK₂ of a-NH3Groupª9.79.08.89.810.89.19.79.69.29.79.69.09.29.110.69.210.49.49.19.6pK₂ of lonizingSide Chainª12.53.98.34.26.010.010.1Residue Mass(daltons)71.08156.20114.11115.09103.14128.14129.1257.06137.15113.17113.17128.18131.21147.1897.1287.08101.11186.21163.1899.14Occurrence inProteins (mol %)8.75.04.25.91.33.76.67.92.45.58.95.52.04.04.75.85.61.53.57.2

Amino acids are the building blocks of proteins and peptides. They have two common functional…

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Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

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Problem 15QP

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Of the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral center
Of the 20 protein-derived amino acids shown in Table 27.1, how many contain Q.) an aromatic ring
Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of this peptide at pH = 1? What is the net charge of this peptide at pH = 14?
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln Which amino acid/s is/are hydrophobic? Which amino acid/s is/are polar uncharged? Which amino acid/s is/are polar charged?
. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids. Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr – Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala – Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
Considering the chemical characteristics of the amino acids valine and glutamic acid (see Figure 5.14), propose a possible explanation for the dramatic effect on protein function that occurs when valine is substituted for glutamic acid.
you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
Identify and encircle the peptide bonds in this polypeptide (Asp-Sec-Leu-Cys-Glu).
The bacterially produced antibiotic gramicidin A forms channels in cell membranes that allow the free diff usion of Na+ and K+ ions, thereby killing the cell. This peptide consists of a sequence of Dand L-amino acids. The sequence of a segment of fi ve amino acids in gramicidin A is R-Gly-L-Ala-D-Leu-L-Ala-D-Val-R′. Complete the Fischer projection below by adding the correct group to each vertical bond.
Which of the following peptides is more likely to take up an α-helical structure, and why?(a) LKAENDEAARAMSEA(b) CRAGGFPWDQPGTSN
Draw Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly peptide. What is the net charge of this peptide at pH 3, 8 and 11? What can you say about pI value of this peptide?

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