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Figure 4 | BMC Structural Biology

Figure 4

From: Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca2+-calmodulin

Figure 4

Main correlated motions of two isoforms of human translation elongation factor 1A. a-i – eEF1A1, j-r – eEF1A2. a-c – 2500–10466 ps of trajectory 2; d-f – 5440–10514 ps of trajectory 4; g-i – 3960–9920 of trajectory 5; j-l – 1070–10000 ps of trajectory 9; m-o – 3780–10417 ps of trajectory 11; p-r – 1130–10197 ps of trajectory 12. a, d, g, j, m, p – first eigenvector; b, e, h, k, n, q – second eigenvector; c, f, i, l, o, r – third eigenvector. The protein regions of the maximal C α -atom displacements (> 0.05 nm) are colored in black. The motions are shown on the average protein conformations in the respective trajectory ranges.

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