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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/10975
Título

A designed protein as experimental model of primordial folding

AutorSadqi, Mourad; Alba, Eva de; Pérez-Jiménez, Raúl; Sánchez-Ruiz, José M.; Muñoz van den Eynde, Víctor
Palabras claveEnergy landscape
Glassy dynamics
Molecular evolution
Protein design
Protein folding
Fecha de publicación24-feb-2009
EditorNational Academy of Sciences (U.S.)
CitaciónProc. Natl. Acad. Sci. USA (PNAS), doi: 10.1073/pnas.0812108106
ResumenHow do proteins accomplish folding during early evolution? Theoretically the mechanism involves the selective stabilization of the native structure against all other competing compact conformations in a process that involves cumulative changes in the amino acid sequence along geological timescales. Thus, an evolved protein folds into a single structure at physiological temperature, but the conformational competition remains latent. For natural proteins such competition should emerge only near cryogenic temperatures, which places it beyond experimental testing. Here, we introduce a designed monomeric miniprotein (FSD-1ss) that within biological temperatures (330–280 K) switches between simple fast folding and highly complex conformational dynamics in a structurally degenerate compact ensemble. Our findings demonstrate the physical basis for protein folding evolution in a designed protein, which exhibits poorly evolved or primordial folding. Furthermore, these results open the door to the experimental exploration of primitive folding and the switching between alternative protein structures that takes place in evolutionary branching points and prion diseases, as well as the benchmarking of de novo design methods.
Descripción6 pages, 4 figures.-- Available Open Access at the publisher's site.-- Article in press.
Supporting information (SI Text, Suppl. figs. S1-S2, Suppl. table S1) available at: http://www.pnas.org/content/suppl/2009/02/24/0812108106.DCSupplemental/0812108106SI.pdf
Versión del editorhttp://dx.doi.org/10.1073/pnas.0812108106
URIhttp://hdl.handle.net/10261/10975
DOI10.1073/pnas.0812108106
ISSN0027-8424
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