de- 1 2 3 5 7 8 9 10 Пе - Ala - His - Thr - Тyr — Gly - Pro - Phe-Glu - Ala- 11 12 13 14 15 16 17 18 19 20 Ala – Mat – Cys – Lys – Trp – Glu – Ala – Gln-Pro – Asp- 21 22 23 24 25 26 27 28 Gly – Met – Glu – Cys – Ala – Phe – His – Arg
de- 1 2 3 5 7 8 9 10 Пе - Ala - His - Thr - Тyr — Gly - Pro - Phe-Glu - Ala- 11 12 13 14 15 16 17 18 19 20 Ala – Mat – 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
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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Question
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.
(a) Where might bends or β turns occur?
(b) Where might intrachain disulfide cross-linkages be formed?
(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.
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