Fig. 9: Analysis of the fluctuations of inter-loop hydrogen bonding networks. | Nature Communications

Fig. 9: Analysis of the fluctuations of inter-loop hydrogen bonding networks.

From: Gating mechanism of elongating β-ketoacyl-ACP synthases

Fig. 9: Analysis of the fluctuations of inter-loop hydrogen bonding networks.The alternative text for this image may have been generated using AI.

Histograms showing the distances between the hydrogen-bond donating Asp265 and highly conversed (hydrogen-bonding accepting) resudes, Gly399, Phe400, Gly401, Gly402, and Asn404 sampled computationally. Histograms of these distances sampled in molecular dynamics (MD) simulations of a apo-FabF, b apo-FabB, c apo-FabF*, d apo-FabB*, e acyl-AcpP·FabF, and f acyl-AcpP·FabB, respectively.

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