The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

PNAS Kühnel et al. 10.1073/pnas.0403069101.

Supporting Information

Files in this Data Supplement:

Supporting Figure 4
Supporting Table 3
Supporting Text




Supporting Figure 4

Fig. 4. DSC spectra of the wild-type and mutant vasodilator-stimulated phosphoprotein (VASP) tetramerization domain (TD) in 1 M guanidine hydrochloride/0.1 M NaCl/0.02 M Mes (pH 6.2). Protein concentrations were 0.5 mg/ml.

 

 

Table 3. Differential scanning calorimetry data

*Unfolding enthalpies obtained by the following two methods are given: the value obtained by fitting to a non-two-state transition model, as well as the value determined from the concentration dependence of midpoint transition temperature.

 

 

 

Supporting Text

DSC Experiments. The unfolding enthalpy D H was determined by two methods (Table 3). First, D H was calculated by fitting the data to a non-two-state model with zero dCp for transition with the origin (version 4.1) software (MicroCal, Northampton, MA). Secondly, the D H value was derived from the concentration dependence of transition temperature. The following equation assuming a tetramer to monomer transition (1) was used:

,

where T_1/2 is the transition temperature, c the concentration of the monomeric protein, D H the unfolding enthalpy, and D S the entropy change of the transition process.

All measurements were done with 0.5 mg/ml protein solutions in 1 M guanidine hydrochloride/100 mM NaCl/20 mM Mes (pH 6.2).

1. Lassalle, M. W., Hinz, H. J., Wenzel, H., Vlassi, M., Kokkinidis, M. & Cesareni, G. (1998) J. Mol. Biol. 279, 987–1000.

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