Abstract
The local hydrophobicity (LHP) around a
residue defined as the sum of hydrophobicity (HP) values of
residues surrounding the residue within a specified distance was
calculated based on the structure of staphylococcal nuclease
(SNase) in the Protein Data Bank. The three-stages (nucleation,
assembly, and stabilization) folding model was assumed to
investigate the effects of LHP in the folding of SNase. Based on
the correlation between HP and LHP, we formulated the correlation
coefficient between LHP and secondary structure at each residue to
estimate the percentage contents of secondary structures from
changes of LHPs in mutants. The estimations are qualitatively and
quantitatively consistent with those from Circular Dichroism
measurements on mutants W140A (Tryptophan at 140 is replaced by
Alanine), F61W/W140A, Y93W/W140A and E75G.
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