Figures and Tables
From the following article:
Dynamic personalities of proteins
Katherine Henzler-Wildman & Dorothee Kern
Nature 450, 964-972(13 December 2007)
doi:10.1038/nature06522
Figure 1
The energy landscape defines the amplitude and timescale of protein motions.
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Figure 2
Microsecond-to-millisecond protein dynamics are necessary for catalysis and are an intrinsic property of CYPA as shown by NMR relaxation dispersion experiments.
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Figure 3
Single-molecule FRET reveals ordered, stepwise rotation of F0F1-ATP synthase on the millisecond timescale during ATP hydrolysis and synthesis.
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Figure 4
Time dependence of carbon-monoxide migration and corresponding structural relaxation in myoglobin, using picosecond time-resolved X-ray crystallography.
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Figure 5
The role of protein dynamics in molecular recognition by calmodulin on a range of timescales.
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Figure 6
Ion-channel selectivity investigated by X-ray crystallography and molecular-dynamics simulations.
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Figure 7
A hierarchy of protein dynamics in space and time underlies enzyme catalysis, using the enzyme adenylate kinase as an example.
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