1J4M
Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)
Summary for 1J4M
Entry DOI | 10.2210/pdb1j4m/pdb |
Related | 1K43 |
Descriptor | MBH12 (1 entity in total) |
Functional Keywords | beta-hairpin, de novo protein |
Total number of polymer chains | 1 |
Total formula weight | 1703.88 |
Authors | Pastor, M.T.,Lopez de la Paz, M.,Lacroix, E.,Serrano, L.,Perez-Paya, E. (deposition date: 2001-10-10, release date: 2001-10-17, Last modification date: 2023-12-27) |
Primary citation | Pastor, M.T.,Lopez de la Paz, M.,Lacroix, E.,Serrano, L.,Perez-Paya, E. Combinatorial approaches: a new tool to search for highly structured beta-hairpin peptides. Proc.Natl.Acad.Sci.USA, 99:614-619, 2002 Cited by PubMed Abstract: Here we present a combinatorial approach to evolve a stable beta-hairpin fold in a linear peptide. Starting with a de novo-designed linear peptide that shows a beta-hairpin structure population of around 30%, we selected four positions to build up a combinatorial library of 20(4) sequences. Deconvolution of the library using circular dichroism reduced such a sequence complexity to 36 defined sequences. Circular dichroism and NMR of these peptides resulted in the identification of two linear 14-aa-long peptides that in plain buffered solutions showed a percentage of beta-hairpin structure higher than 70%. Our results show how combinatorial approaches can be used to obtain highly structured peptide sequences that could be used as templates in which functionality can be introduced. PubMed: 11782528DOI: 10.1073/pnas.012583999 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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