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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Key interaction networks : Identifying evolutionarily conserved non-covalent interaction networks across protein families

Author

  • Dariia Yehorova
  • Rory M Crean
  • Peter M Kasson
  • Shina C L Kamerlin

Summary, in English

Protein structure (and thus function) is dictated by non-covalent interaction networks. These can be highly evolutionarily conserved across protein families, the members of which can diverge in sequence and evolutionary history. Here we present KIN, a tool to identify and analyze conserved non-covalent interaction networks across evolutionarily related groups of proteins. KIN is available for download under a GNU General Public License, version 2, from https://www.github.com/kamerlinlab/KIN. KIN can operate on experimentally determined structures, predicted structures, or molecular dynamics trajectories, providing insight into both conserved and missing interactions across evolutionarily related proteins. This provides useful insight both into protein evolution, as well as a tool that can be exploited for protein engineering efforts. As a showcase system, we demonstrate applications of this tool to understanding the evolutionary-relevant conserved interaction networks across the class A β-lactamases.

Publishing year

2024-03

Language

English

Publication/Series

Protein Science

Volume

33

Issue

3

Document type

Journal article

Publisher

The Protein Society

Keywords

  • Algorithms
  • Proteins/chemistry

Status

Published

ISBN/ISSN/Other

  • ISSN: 1469-896X