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. Author manuscript; available in PMC: 2010 Nov 3.
Published in final edited form as: Proteins. 2009 May 15;75(3):610–627. doi: 10.1002/prot.22273

Table 3.

Characterization of the TRX homologs used in this report.

Source Tm1 Cpmax2 Hyst.3 Gbar4 θnat5 θTS θ unf θRP

E. coli 359 13.9 10.0 0.6 0.9 1.8 2.2 1.2
S. aureus 343 11.3 9.9 1.2 1.2 1.6 2.1 1.2
Spinach-m cholorplast 349 11.1 18.8 1.0 1.3 1.7 2.2 1.3
Anabaena sp. 366 25.3 62.8 5.4 1.0 1.6 2.4 1.4
Human mitochondria 376 21.3 61.0 2.5 1.1 1.7 2.2 1.3
C. reinhardtii cytosol 385 20.4 67.9 5.1 1.1 1.7 2.3 1.3
Spinach-f cholorplast 366 7.9 9.0 0.4 1.5 1.8 2.3 1.4
Fruit fly cytosol 379 15.6 30.0 1.9 1.3 1.9 2.5 1.4
Human cytosol 369 19.9 52.9 3.6 1.2 1.7 2.4 1.3

Average 365.8 16.3 35.8 2.4 1.2 1.7 2.3 1.3
Standard deviation 13.7 5.8 25.2 1.9 0.2 0.1 0.1 0.1
1

Melting temperature (K).

2

Peak height of the heat capacity curve in units of kcal/mol·K.

3

Hysteresis temperature range (K).

4

The height of the straddling free energy barrier (units are kcal/mol) separating the native and unfolded basins within the one-dimensional free energy landscapes.

5

Key points along the one-dimensional free energy landscape at the respective Tm are provided: θnat ≡ minimum of the native free energy basin, θTS ≡ location of the transition state barrier, θunf ≡ the minimum of the unfolded free energy basin, and θRP ≡ rigid cluster percolation threshold.