On methods for determining solvent accessible surface area for proteins in their unfolded state

BMC Research Notes

Table 2 R-squared values using change in ASA values

Response variable	Tripeptide R^2	ProtSA static	ProtSA	Upper creamer	Avg creamer	Lower creamer	Avg gong/rose	Lower gong/rose
Nres	.9945	.9936	.9932	.9958	.9945	.9921	.9934	.9954
∆C_p	.7857	.7801	.7797	.7815	.78	.7772	.7777	.7838
∆H(60)	.8034	.7909	.7951	.7944	.7943	.7937	.8087	.7982
∆S(60)	.7707	.7665	.7663	.7655	.7661	.7666	.7776	.7685
∆H*	.937	.9263	.9296	.93	.9292	.9275	.9365	.9331
∆S*	.9344	.928	.929	.9295	.929	.9278	.9343	.9321

R-squared values are from regressions using each unfolded surface area method to predict the six different response variables from Robertson and Murphy [11]: number of residues (Nres), heat capacity change upon unfolding (∆C_p), enthalpy of unfolding at 60 degrees C (∆H(60)) and at 100 degrees C (∆H*), and entropy of unfolding at 60 degrees C (ΔS(60)) and at 112 degrees C (∆S*). Values in bold are either improvements, ties, or in the closest three to the performance of the tripeptide method in terms of R-squared values. Tripeptide reference values are in italics.

ISSN: 1756-0500