2N4N
NMR structure for a 3-stranded parallel beta-sheet
Summary for 2N4N
| Entry DOI | 10.2210/pdb2n4n/pdb |
| NMR Information | BMRB: 25673 |
| Descriptor | DESIGNED BETA SHEET (1 entity in total) |
| Functional Keywords | de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 2877.45 |
| Authors | Kung, V.M.,Cornilescu, G.,Gellman, S.H. (deposition date: 2015-06-24, release date: 2015-10-28, Last modification date: 2024-11-27) |
| Primary citation | Kung, V.M.,Cornilescu, G.,Gellman, S.H. Impact of Strand Number on Parallel beta-Sheet Stability. Angew.Chem.Int.Ed.Engl., 54:14336-14339, 2015 Cited by PubMed Abstract: We have examined whether parallel β-sheet secondary structure becomes more stable as the number of β-strands increases, via comparisons among peptides designed to adopt two- or three-stranded parallel β-sheet conformations in aqueous solution. Our three-strand design is the first experimental model of a triple-stranded parallel β-sheet. Analysis of the designed peptides by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of β-strands, from two to three, increases the stability of the parallel β-sheet. We present the first experimental evidence for cooperativity in the folding of a triple-stranded parallel β-sheet, and we show how minimal model systems may enable experimental documentation of characteristic properties, such as CD spectra, of parallel β-sheets. PubMed: 26457984DOI: 10.1002/anie.201506448 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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