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Comparative analysis of permanent and transient domain–domain interactions in multi-domain proteins

Sidhanta, SPD and Sowdhamini, R and Srinivasan, N (2023) Comparative analysis of permanent and transient domain–domain interactions in multi-domain proteins. In: Proteins: Structure, Function and Bioinformatics .

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Official URL: https://doi.org/10.1002/prot.26581


Protein domains are structural, functional, and evolutionary units. These domains bring out the diversity of functionality by means of interactions with other co-existing domains and provide stability. Hence, it is important to study intra-protein inter-domain interactions from the perspective of types of interactions. Domains within a chain could interact over short timeframes or permanently, rather like protein–protein interactions (PPIs). However, no systematic study has been carried out between two classes, namely permanent and transient domain–domain interactions. In this work, we studied 263 two-domain proteins, belonging to either of these classes and their interfaces on the basis of several factors, such as interface area and details of interactions (number, strength, and types of interactions). We also characterized them based on residue conservation at the interface, correlation of residue motions across domains, its involvement in repeat formation, and their involvement in particular molecular processes. Finally, we could analyze the interactions arising from domains in two-domain monomeric proteins, and we observed significant differences between these two classes of domain interactions and a few similarities. This study will help to obtain a better understanding of structure–function and folding principles of multi-domain proteins. © 2023 Wiley Periodicals LLC.

Item Type: Journal Article
Publication: Proteins: Structure, Function and Bioinformatics
Publisher: John Wiley and Sons Inc
Additional Information: The copyright for this article belongs to the Authors.
Keywords: domain repeats, hydrophobic interactions, multi-domain proteins, normal mode analysis, proteinfolds, residue conservation
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 18 Dec 2023 03:37
Last Modified: 18 Dec 2023 03:37
URI: https://eprints.iisc.ac.in/id/eprint/83495

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