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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Journal of chemical information and modeling

Extracting Dynamical Correlations and Identifying Key Residues for Allosteric Communication in Proteins by correlationplus.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of chemical information and modeling - 25 Oct 2021

Tekpinar M, Neron B, Delarue M

Link to Pubmed [PMID] – 34652149

Link to HAL – Click here

Link to DOI – 10.1021/acs.jcim.1c00742

J Chem Inf Model 2021 Oct; 61(10): 4832-4838

Extracting dynamical pairwise correlations and identifying key residues from large molecular dynamics trajectories or normal-mode analysis of coarse-grained models are important for explaining various processes like ligand binding, mutational effects, and long-distance interactions. Efficient and flexible tools to perform this task can provide new insights about residues involved in allosteric regulation and protein function. In addition, combining and comparing dynamical coupling information with sequence coevolution data can help to understand better protein function. To this aim, we developed a Python package called correlationplus to calculate, visualize, and analyze pairwise correlations. In this way, the package aids to identify key residues and interactions in proteins. The source code of correlationplus is available under LGPL version 3 at https://github.com/tekpinar/correlationplus. The current version of the package (0.2.0) can be installed with common installation methods like conda or pip in addition to source code installation. Moreover, docker images are also available for usage of the code without installation.