English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/213361
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 | DATACITE
Exportar a otros formatos:


Global Changes in Local Protein Dynamics Reduce the Entropic Cost of Carbohydrate Binding in the Arabinose-binding Protein

AuthorsMacRaild, Christopher A.; Hernández Daranas, Antonio ; Bronowska, Agnieszka; Homans, Steve W.
KeywordsLigand binding
NMR relaxation
Molecular dynamics
Periplasmic binding protein
Issue Date4-May-2007
CitationJournal of Molecular Biology 368(3): 822-832 (2007)
AbstractProtein dynamics make important but poorly understood contributions to molecular recognition phenomena. To address this, we measure changes in fast protein dynamics that accompany the interaction of the arabinose-binding protein (ABP) with its ligand, d-galactose, using NMR relaxation and molecular dynamics simulation. These two approaches present an entirely consistent view of the dynamic changes that occur in the protein backbone upon ligand binding. Increases in the amplitude of motions are observed throughout the protein, with the exception of a few residues in the binding site, which show restriction of dynamics. These counter-intuitive results imply that a localised binding event causes a global increase in the extent of protein dynamics on the pico- to nanosecond timescale. This global dynamic change constitutes a substantial favourable entropic contribution to the free energy of ligand binding. These results suggest that the structure and dynamics of ABP may be adapted to exploit dynamic changes to reduce the entropic costs of binding.
Publisher version (URL)https://doi.org/10.1016/j.jmb.2007.02.055
Appears in Collections:(IPNA) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdfArtículo principal16,34 kBAdobe PDFThumbnail
Show full item record
Review this work

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