Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.

The Journal of Biological Chemistry
J FunahashiK Yutani

Abstract

Water molecules make a hydration structure with the network of hydrogen bonds, covering on the surface of proteins. To quantitatively estimate the contribution of the hydration structure to protein stability, a series of hydrophilic mutant human lysozymes (Val to Ser, Tyr, Asp, Asn, and Arg) modified at three different positions on the surface, which are located in the alpha-helix (Val-110), the beta-sheet (Val-2), and the loop (Val-74), were constructed. Their thermodynamic parameters of denaturation and crystal structures were examined by calorimetry and by x-ray crystallography at 100 K, respectively. The introduced polar residues made hydrogen bonds with protein atoms and/or water molecules, sometimes changing the hydration structure around the mutation site. Changes in the stability of the mutant proteins can be evaluated by a unique equation that considers the conformational changes resulting from the substitutions. Using this analysis, the relationship between the changes in the stabilities and the hydration structures for mutant human lysozymes substituted on the surface could be quantitatively estimated. The analysis indicated that the hydration structure on protein surface plays an important role in determining the co...Continue Reading

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Citations

Oct 9, 2007·Bioinformatics·Chris Deutsch, Bala Krishnamoorthy
Nov 23, 2006·Biophysical Chemistry·Liang-Tsung HuangM Michael Gromiha
Mar 21, 2003·Protein Engineering·Kazufumi TakanoKatsuhide Yutani
Oct 4, 2006·Physiological Reviews·Michael J Page, Enrico Di Cera
Apr 24, 2003·The Journal of Biological Chemistry·Gennaro EspositoVittorio Bellotti
Nov 4, 2005·The Journal of Biological Chemistry·Enrico Di Cera
Jul 16, 2017·The Journal of Biological Chemistry·Aron BroomElizabeth M Meiering
Jun 12, 2020·Journal of Structural Biology·Mathilde Carpentier, Jacques Chomilier
Sep 25, 2017·The Journal of Physical Chemistry Letters·Antonio Benedetto

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