English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/19310
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Use of constrained synthetic amino acids in β-Helix proteins for conformational control

AuthorsZanuy, David; Jiménez, Ana I. ; Cativiela, Carlos ; Nussinov, Ruth; Alemán, Carlos
Issue DateMar-2007
PublisherAmerican Chemical Society
CitationJournal of Physical Chemistry B 111(12): 3236-3242 (2007)
AbstractA highly constrained amino acid has been introduced in the turn region of a β-helix to increase the conformational stability of the native fold for nanotechnological purposes. The influence of this specific amino acid replacement in the final organization of β-helix motifs has been evaluated by combining ab initio first-principles calculations on model systems and molecular dynamics simulations of entire peptide segments. The former methodology, which has been applied to a sequence containing three amino acids, has been used to develop adjusted templates. Calculations indicated that 1-amino-2,2-diphenylcyclopropanecarboxylic acid, a constrained cyclopropane analogue of phenylalanine, exhibits a strong tendency to form and promote folded conformations. On the other hand, molecular dynamics simulations are employed to probe the ability of such a synthetic amino acid to enhance the conformational stability of the β-helix motif, which is the first requirement for further protein nanoengineering. A highly regular segment from a naturally occurring β-helix protein was selected as a potential nanoconstruct module. Simulations of wild type and mutated segments revealed that the ability of the phenylalanine analogue to nucleate turn conformations enhances the conformational stability of the β-helix motif in isolated peptide segments.
Description7 pages, 4 figures, 1 table.
Publisher version (URL)http://dx.doi.org/10.1021/jp065025k
Appears in Collections:(ICMA) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.