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Article

Multiple molecular dynamics simulations of TEM beta-lactamase: dynamics and water binding of the omega-loop.

Biophysical journal - 4 Nov 2009

Bös Fabian, Pleiss Jürgen

Abstract excerpt

The Omega-loop of TEM beta-lactamase is involved in substrate recognition and catalysis. Its dynamical properties and interaction with water molecules were investigated by performing multiple molecular dynamics simulations of up to 50 ns. Protein flexibility was assessed by calculating the root mean-square fluctuations and the generalized order parameter, S(2). The residues in secondary structure elements are...

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Identifiers

PMID: 19883598
DOI: 10.1016/j.bpj.2009.08.031
PMCID: PMC2770601

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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