%0 Book Section %1 statphys23_0868 %A Wu, M.C. %A Hu, C.K. %A Chen, H.M. %A Tsong, T.Y. %B Abstract Book of the XXIII IUPAP International Conference on Statistical Physics %C Genova, Italy %D 2007 %E Pietronero, Luciano %E Loreto, Vittorio %E Zapperi, Stefano %K decomposition empirical folding hydrophobicity local mode model nuclease staphylococcal statphys23 three-stages topic-10 %T Local hydrophobicity in protein folding: Theoretical model and experimental test with staphylococcal nuclease and its mutants %U http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=868 %X 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.

@incollection{statphys23_0868, 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.}, added-at = {2007-06-20T10:16:09.000+0200}, address = {Genova, Italy}, author = {Wu, M.C. and Hu, C.K. and Chen, H.M. and Tsong, T.Y.}, biburl = {https://www.bibsonomy.org/bibtex/2af3e61c4bf935034f41a34abcfe9a86f/statphys23}, booktitle = {Abstract Book of the XXIII IUPAP International Conference on Statistical Physics}, editor = {Pietronero, Luciano and Loreto, Vittorio and Zapperi, Stefano}, interhash = {bb81d21ed7b9fd6ebed5bc4b78c3bedc}, intrahash = {af3e61c4bf935034f41a34abcfe9a86f}, keywords = {decomposition empirical folding hydrophobicity local mode model nuclease staphylococcal statphys23 three-stages topic-10}, month = {9-13 July}, timestamp = {2007-06-20T10:16:31.000+0200}, title = {Local hydrophobicity in protein folding: Theoretical model and experimental test with staphylococcal nuclease and its mutants}, url = {http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=868}, year = 2007 }