14-helical folding in a cyclobutane-containing beta-tetrapeptide
Author | dc.contributor.author | Izquierdo, S. | |
Author | dc.contributor.author | Kogan Bocian, Marcelo | es_CL |
Author | dc.contributor.author | Parella, T. | es_CL |
Author | dc.contributor.author | Moglioni, A. G. | es_CL |
Author | dc.contributor.author | Branchadell, V. | es_CL |
Author | dc.contributor.author | Giralt, Ernest | es_CL |
Author | dc.contributor.author | Ortuño, R. M. | es_CL |
Admission date | dc.date.accessioned | 2011-04-07T12:52:06Z | |
Available date | dc.date.available | 2011-04-07T12:52:06Z | |
Publication date | dc.date.issued | 2004-07-23 | |
Cita de ítem | dc.identifier.citation | JOURNAL OF ORGANIC CHEMISTRY 69 (15): 5093-5099 | en_US |
Identifier | dc.identifier.issn | 0022-3263 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/121162 | |
Abstract | dc.description.abstract | The efficient synthesis of tetrapeptide 5 containing, in alternation, cyclobutane and beta-alanine residues is described. NMR experiments both at low temperature in CDCl3 and at 298 K in DMSOd(6) solutions show the contribution of a strong hydrogen bond in the folded major conformation of 5. Temperature coefficients and diffusion times point out a hydrogen bond involving the NH proton from the cyclobutane residue 1 whereas NOES manifest the high rigidity of the central fragment of the molecule and are compatible with a 14-membered macrocycle. Theoretical calculations predict a most stable folded conformation corresponding to a 14-helix stabilized by a hydrogen bond between NH10 in the first residue and OC25 in the third residue. This structure remains unaltered during the molecular dynamics simulation at 298 K in chloroform. All these results provide evidence for a 14-helical folding and reveal the ability of cis-2-aminocyclobutane carboxylic acid residues to promote folded conformations when incorporated into beta-peptides. | en_US |
Lenguage | dc.language.iso | en | en_US |
Publisher | dc.publisher | AMER CHEMICAL SOC | en_US |
Keywords | dc.subject | HELICAL SECONDARY STRUCTURE | en_US |
Título | dc.title | 14-helical folding in a cyclobutane-containing beta-tetrapeptide | en_US |
Document type | dc.type | Artículo de revista |
Files in this item
This item appears in the following Collection(s)
-
Artículos de revistas
Artículos de revistas