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Delineating the Role of mutation on the structural stability and conformational landscape of inhibitor-resistant TEMβ-lactamase: A high-performance molecular dynamics simulations Study

2024-01-30

Abstract excerpt

The gain of function mutations and structural adjustment towards β-lactamase inhibitors in TEM-type β-lactamase among the uropathogenic E.coli (UPEC) culminates into treatment complications and demands a detailed investigation. In this study, uncharacterized amino acid substitutions, M69L/I84V/W165G/V184A/V262I/N276S in inhibitor-resistant TEM (IRT) β-lactamase isolated from clinical UPEC were subjected to extensi...

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Literature Corpus work
5685abcd-5279-5cbb-af00-c2b13a1526a5
DOI
10.22541/au.170665125.55483763/v1
Open publication

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Delineating the Role of mutation on the structural stability and conformational landscape of inhibitor-resistant TEMβ-lactamase: A high-performance molecular dynamics simulations StudyDOI 10.22541/au.170665125.55483763/v1
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