Download PDF by Raphael Guerois, Manuela López de la Paz: Protein Design (Methods in Molecular Biology)

By Raphael Guerois, Manuela López de la Paz

ISBN-10: 1588295850

ISBN-13: 9781588295859

Protein layout: tools and functions provides the main updated protein layout and engineering techniques in order that readers can adopt their very own initiatives with a greatest likelihood of luck. The authors current built-in computational methods that require a variety of levels of computational complexity, and the foremost accomplishments which were accomplished within the layout and structural characterization of helical peptides and proteins.

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And Matthews, B. W. (1992) Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. Biochemistry 31, 3590–3596. 13. , and Baldwin, R. (1993) Helix capping propensities in peptides parallel those in proteins. Proc. Natl. Acad. Sci. USA 90, 11332–11336. 14. , Feliciano, E. , and Nambiar, K. P. (1993) Stabilization of alphahelical structures in short peptides via end capping. Proc. Natl. Acad. Sci. USA 90, 838–842. 15. Dasgupta, S.

Designed three-stranded β-sheets have three to seven residues per strand. 2. ), the selection of an adequate βturn sequence is crucial to ensure that the designed peptide will adopt the target β-hairpin. Table 1 has been built using β-turn positional potentials statistically derived from protein structures (22). Table 1 is very useful in selecting the βturn residues by taking into account which is the most appropriate turn for the desired β-hairpin, namely type I for 3:5 and 4:4 β-hairpins, and type I' or II' for 2:2 β-hairpins.

I. (2003) Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the α-helix have the same helical propensity. Protein Sci. 12, 1169–1176. 109. Thomas, S. , Loladze, V. , and Makhatadze, G. I. (2001) Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of α-helices. Proc. Nat. Acad. Sci. USA 98, 10670–10675. 110. , Olson, C. , Bell, A. , and Kallenbach, N. R. O H-bonding between Phe and Glu side chains in α-helical peptides.

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Protein Design (Methods in Molecular Biology) by Raphael Guerois, Manuela López de la Paz

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