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Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on amino acid sequence data. Consider the amino acid sequence. 1 2 3 4 6. 7 8 9. 10 lle – Ala - His - Thr – Tyr – Gly –Pro –Phe - Glu – Ala 11 12 13 14 15 16 17 18 19 20 Ala – Met – Cys – Lys – Trp – Glu – Ala – Gln – Pro – Asp – | 21 22 23 24 25 26 27 28 Gly –Met – Glu – Cys – Ala -Phe – His – Arg

Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on amino acid sequence data. Consider the amino acid sequence. 1 2 3 4 6. 7 8 9. 10 lle – Ala - His - Thr – Tyr – Gly –Pro –Phe - Glu – Ala 11 12 13 14 15 16 17 18 19 20 Ala – Met – Cys – Lys – Trp – Glu – Ala – Gln – Pro – Asp – | 21 22 23 24 25 26 27 28 Gly –Met – Glu – Cys – Ala -Phe – His – Arg

Biochemistry
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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Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on amino acid sequence data. Consider the amino acid sequence. 1 2 3 4 5 9. 10 Ile – Ala - His Thr – Tyr – Gly –Pro –Phe – Glu – Ala 11 12 13 14 15 16 17 18 19 20 Ala -Met – Cys – Lys – Trp – Glu – Ala – Gln –Pro – Asp – 21 22 23 24 25 26 27 28 Gly – Met – Glu – Cys – Ala –Phe – His – Arg Where might bends or ß turns occur? Where might intrachain disulfide cross-linkages form? residues 14 and 16 between residues 4 and 18 residues 7 and 19 between residues 12 and 22 residues 9 and 19 between residues 13 and 24 between residues 14 and 16 residues 10 and 11
Transcribed Image Text:Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on amino acid sequence data. Consider the amino acid sequence. 1 2 3 4 5 9. 10 Ile – Ala - His Thr – Tyr – Gly –Pro –Phe – Glu – Ala 11 12 13 14 15 16 17 18 19 20 Ala -Met – Cys – Lys – Trp – Glu – Ala – Gln –Pro – Asp – 21 22 23 24 25 26 27 28 Gly – Met – Glu – Cys – Ala –Phe – His – Arg Where might bends or ß turns occur? Where might intrachain disulfide cross-linkages form? residues 14 and 16 between residues 4 and 18 residues 7 and 19 between residues 12 and 22 residues 9 and 19 between residues 13 and 24 between residues 14 and 16 residues 10 and 11
Suppose that the sequence is part of a larger globular protein. Consider the probable location, either on the external surface Which statements correctly describe the probable or the interior of the protein, of each of the amino locations of the amino acids? acid residues. Ala is located on the external surface of the protein because it is polar. The table gives the hydropathy index values for selected amino acids in the peptide. Thr is polar and can be located on the external surface or in the interior of the protein. Amino acid Hydropathy index Asp is located on the external surface of the protein because it is charged. alanine 1.8 isoleucine 4.5 Gln is located in the interior of the protein because it is uncharged. Ile and Lys are located in the interior of the protein because they are not polar. threonine -0.7 glutamine -3.5 lysine -3.9 aspartate -3.5
Transcribed Image Text:Suppose that the sequence is part of a larger globular protein. Consider the probable location, either on the external surface Which statements correctly describe the probable or the interior of the protein, of each of the amino locations of the amino acids? acid residues. Ala is located on the external surface of the protein because it is polar. The table gives the hydropathy index values for selected amino acids in the peptide. Thr is polar and can be located on the external surface or in the interior of the protein. Amino acid Hydropathy index Asp is located on the external surface of the protein because it is charged. alanine 1.8 isoleucine 4.5 Gln is located in the interior of the protein because it is uncharged. Ile and Lys are located in the interior of the protein because they are not polar. threonine -0.7 glutamine -3.5 lysine -3.9 aspartate -3.5
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