Global Changes in Local Protein Dynamics Reduce the Entropic Cost of Carbohydrate Binding in the Arabinose-binding Protein
Protein 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.
Main Authors: | MacRaild, Christopher A., Hernández Daranas, Antonio, Bronowska, Agnieszka, Homans, Steve W. |
---|---|
Format: | artículo biblioteca |
Language: | English |
Published: |
Elsevier
2007-05-04
|
Subjects: | Ligand binding, Thermodynamics, NMR relaxation, Molecular dynamics, Periplasmic binding protein, |
Online Access: | http://hdl.handle.net/10261/213361 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Letter to the Editor: Backbone Resonance Assignment of the L-Arabinose Binding Protein in Complex with D-Galactose
by: Hernández Daranas, Antonio, et al.
Published: (2004-04-14) -
Thermodynamics of Binding of d-Galactose and Deoxy Derivatives thereof to the l-Arabinose-binding Protein
by: Hernández Daranas, Antonio, et al.
Published: (2004-09-01) -
Binding affinity prediction using a nonparametric regression model based on physicochemical and structural descriptors of the nano-environment for protein-ligand interactions.
by: BORRO, L., et al.
Published: (2017-01-17) -
Changes in the structure and protein binding ability of condensed tannins during decomposition of fresh needles and leaves
by: Maie, Nagamitsu, et al.
Published: (2003-04) -
Unexpected thermodynamic signature for the interaction of hydroxymethylated DNA with MeCP2
by: Ortega-Alarcón, David, et al.
Published: (2023-03-31)