2K6R
Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics and structural frustration
Summary for 2K6R
| Entry DOI | 10.2210/pdb2k6r/pdb |
| Related | 1FME 1FSV |
| NMR Information | BMRB: 15879 |
| Descriptor | Full Sequence Design 1 Synthetic Superstable (1 entity in total) |
| Functional Keywords | synthetic protein, non-natural amino acids, de novo protein design, rugged folding energy landscape, structural frustration, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 3854.42 |
| Authors | Sadqi, M.,de Alba, E.,Perez-Jimenez, R.,Sanchez-Ruiz, J.M.,Munoz, V. (deposition date: 2008-07-18, release date: 2009-06-16, Last modification date: 2025-03-26) |
| Primary citation | Sadqi, M.,de Alba, E.,Perez-Jimenez, R.,Sanchez-Ruiz, J.M.,Munoz, V. A designed protein as experimental model of primordial folding Proc.Natl.Acad.Sci.USA, 106:4127-4132, 2009 Cited by PubMed Abstract: How 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. PubMed: 19240216DOI: 10.1073/pnas.0812108106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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