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Protein J. 2007 Sep;26(6):395-402.

The correlation of cold denaturation temperature with surface stability factor of proteins.

Author information

1
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.

Abstract

Cold denaturation is an intriguing phenomenon in protein denaturation for elucidating protein accessible surface area (ASA). Compared to the impact of protein surface, the importance of protein-water interactions in cold denaturation may be ruled out significantly. Here, based on the ASA, we have defined a new factor, the surface stability factor (SSF). From the SSF, in combination with the cold denaturation temperature (T(g')) or temperature at DeltaS = 0 (T(s)) of a given protein, one can predict the percent of hydrophobic surface area (H), percent of total surface there on positive and negative charge sum (effective charge) be zero (C), percent of patches hydrophobicity (HP) and others critical surface parameters without any need to the crystallographic data.

PMID:
17503164
DOI:
10.1007/s10930-007-9079-y
[Indexed for MEDLINE]

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