Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
a) From the chemical structure above, write the amino acid sequence using both three-letter and one-letter abbreviations. Disregard chirality for this question.
b) Indicate adjacent to the alpha-carbon of each residue whether it has an L- or D-configuration.
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Follow-up Question
How do you identify the N vs C terminals? For the first part of the question, do you then list the amino acids in order clockwise from N terminal to C terminal?
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Follow-up Question
How do you identify the N vs C terminals? For the first part of the question, do you then list the amino acids in order clockwise from N terminal to C terminal?
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- Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.arrow_forwardThe bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) which side do you expect to face the solvent? Briefly explain your reasons NH, но Nterminusarrow_forwardIdentify the 20 amino acids and their corresponding three-letter and one-letter abbreviationsarrow_forward
- с" CH2 CH2 "НaN H с. CH С" CH Нзс CHз ZI о-оarrow_forwardConsider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.arrow_forwardThere is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!arrow_forward
- Proline is one of the amino acids in the "special" groups of sidechains. One reason for this is the dramatic impact it can have on secondary structure. a) draw the lewis structure for a tripeptide with the sequence Ala-Pro-Ala b) Proline residues are rarely found in alpha helices - in fact, they are often referred to as helix-disrupting amino acids. Thinking about intermolecular interactions, provide an explanation for why proline might disrupt alpha-helices. c) Proline also has a similar effect on beta-sheets, and is rarely found in the middle of beta sheets. Thinking about noncovalent interactions, provide an explanation for why proline might disrupt beta-sheets.arrow_forwardConsider an amino acid (A) with no ionizable side chains, and call the three species involved in the acid/base equilibria H2A+, HA, and A- (see scheme below). Assume that pKa(1) = 2.0 and that pKa(2) = 9.0. Suppose that the total concentration of the amino acid is 1.0 mM. Report to two significant digits. pH [H2A+] (mM) [HA] (mM) [A-] (mM) 1.0 2.0 3.0 4.0 5.0 6.0 7.0 8.0 9.0 10.0 11.0 12.0arrow_forwardcan u help mearrow_forward
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