Related Experiment Video
Updated: Jul 3, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
Networks of coupled rotators: relationship between structures and internal dynamics in metal-binding proteins.
Anne Dhulesia1, Daniel Abergel, Geoffrey Bodenhausen
1Département de Chimie, Ecole Normale Supérieure, 24, rue Lhomond, 75231 Paris Cedex 05, France.
Abstract:
This article presents an analysis of the internal dynamics of the Ca2+-binding protein calbindin, based on the Networks of Coupled Rotators (NCRs) introduced recently. Several fundamental and practical issues raised by this approach are investigated. The roles of various parameters of the model are examined. The NCR model is shown to account for the modifications of the internal dynamics upon Ca2+ binding by calbindin. Two alternative strategies to estimate local internal effective correlation times of the protein are proposed, which offer good agreement between predictions and experiment.
More Related Videos
09:30Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
Published on: August 6, 2018
10:01Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
Published on: June 23, 2026
Related Concept Videos
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Ligand Binding and Linkage
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Structure of Cadherins