Exploring complexity of class-A Beta-lactamase family using physiochemical-based multiplex networks.

ABSTRACT: The Beta-lactamase protein family is vital in countering Beta-lactam antibiotics, a widely used antimicrobial. To enhance our understanding of this family, we adopted a novel approach employing a multiplex network representation of its multiple sequence alignment. Each network layer, derived from the physiochemical properties of amino acids, unveils distinct insights into the intricate interactions among nodes, thereby enabling the identification of key motifs. Nodes with identical property signs tend to aggregate, providing evidence of the presence of consequential functional and evolutionary constraints shaping the Beta-lactamase family. We further investigate the distribution of evolutionary links across various layers. We observe that polarity manifests the highest number of unique lin

SUBMITTER: Bhadola P 

PROVIDER: S-EPMC10667273 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature