By Raphael Guerois, Manuela López de la Paz
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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Additional resources for Protein Design (Methods in Molecular Biology)
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.
Protein Design (Methods in Molecular Biology) by Raphael Guerois, Manuela López de la Paz