Detalle de: Principles for designing proteins with cavities formed by curved β sheets
| Title | Principles for designing proteins with cavities formed by curved β sheets |
| Abstract |
Designing proteins with cavities In de novo protein design, creating custom-tailored binding sites is a particular challenge because these sites often involve nonideal backbone structures. For example, curved b sheets are a common ligand binding motif. Marcos et al. investigated the principles that drive β-sheet curvature by studying the geometry of β sheets in natural proteins and folding simulations. In a step toward custom design of enzyme catalysts, they used these principles to control β-sheet geometry and design proteins with differently shaped cavities. Science , this issue p. 201 |
| Apa Reference | Marcos, E., Basanta, B., Chidyausiku, T.M., Tang, Y., Oberdorfer, G., Liu, G., Swapna, G.V.T., Guan, R., Silva, D., Dou, J., Pereira, J.H., Xiao, R., Sankaran, B., Zwart, P.H., Montelione, G.T. & Baker, D. (2017). Principles for designing proteins with cavities formed by curved β sheets. Science, 355(6321), 201-206. 10.1126/science.aah7389 |
| Doi | 10.1126/science.aah7389 |
| Publication Date | 13 Jan 2017 |
| Publication Type | Article |
| Researcher | Enrique Marcos Benteo |
| Ontology | Computational models and simulations, Sequence analysis, Molecular Interactions/Docking, Protein/Nucleic Acid design |
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