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From the following article:

Solution structure of a protein denatured state and folding intermediate

T. L. Religa, J. S. Markson, U. Mayor, S. M. V. Freund & A. R. Fersht

Nature 437, 1053-1056(13 October 2005)

doi:10.1038/nature04054

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Figure 1 - Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact npg@nature.com

Figure 1

Structure of En-HD L16A at low ionic strength and summary of sequential NOEs and secondary chemical shift values (Protein Data Bank code 1ZTR).

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Figure 2

Backbone dynamics of wild-type and En-HD L16A protein.

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Figure 3

Effects of salt on the properties of wild-type En-HD and L16A, and the difficulties of distinguishing between cooperative and non-cooperative transitions.

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Figure 4

Relaxation kinetics of wild-type En-HD and the L16A mutant at various concentrations of NaCl as a function of temperature at 50 mM NaAc, pH 5.7.

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