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


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 conformational stability of the protein. Study holds ProTherm entries: 15282, 15283, 15284, 15285, 15286, 15287, 15288, 15289, 15290, 15291, 15292, 15293, 15294, 15295, 15296, 15297, 15298, 15299, 15300, 15301, 15302, 15303, 15304, 15305, 15306, 15307, 15308, 15309, 15310, 15311, 15312, 15313, 15314, 15315, 15316, 15317, 15318, 15319, 15320, 15321, 15322, 15323, 15324, 15325, 15326, 15327, 15328, 15329, 15330, 15331, 15332, 15333, 15334, 15335, 15336, 15337, 15338, 15339, 15340, 15341, 15342, 15343, 15344, 15345, 15346, 15347, 15348, 15349, 15350, 15351, 15352, 15353, 15354, 15355, 15356, 15357, 15358, 15359, 15360, 15361, 15362, 15363, 15364, 15365, 15366, 15367, 15368, 15369, 15370, 15371, 15372, 15373 Extra Details: hydration structure; surface; alpha-helix; beta-sheet;

Submission Details

ID: gSPsC2ZW4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:46 p.m.

Version: 1

Publication Details
Funahashi J;Takano K;Yamagata Y;Yutani K,J. Biol. Chem. (2002) Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. PMID:11927576
Additional Information

Study Summary

Number of data points 260
Proteins Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C ; Lysozyme C
Unique complexes 15
Assays/Quantities/Protocols Experimental Assay: dCp temp:64.9 C ; Experimental Assay: dHcal pH:2.7, temp:64.9 C ; Experimental Assay: ddG ; Experimental Assay: dTm ; Experimental Assay: dCp ; Experimental Assay: dHcal pH:2.7 ; Experimental Assay: Tm pH:2.7 ; Experimental Assay: dHcal pH:2.8 ; Experimental Assay: Tm pH:2.8 ; Experimental Assay: dHvH pH:2.8 ; Experimental Assay: dHcal pH:2.72 ; Experimental Assay: Tm pH:2.72 ; Experimental Assay: dHvH pH:2.72 ; Experimental Assay: dHcal pH:3.04 ; Experimental Assay: Tm pH:3.04 ; Experimental Assay: dHvH pH:3.04 ; Experimental Assay: dHcal pH:2.64 ; Experimental Assay: Tm pH:2.64 ; Experimental Assay: dHvH pH:2.64 ; Experimental Assay: dHcal pH:3.34 ; Experimental Assay: Tm pH:3.34 ; Experimental Assay: dHvH pH:3.34 ; Experimental Assay: dHcal pH:3.13 ; Experimental Assay: Tm pH:3.13 ; Experimental Assay: dHvH pH:3.13 ; Experimental Assay: dHcal pH:2.63 ; Experimental Assay: Tm pH:2.63 ; Experimental Assay: dHvH pH:2.63 ; Experimental Assay: dHcal pH:3.38 ; Experimental Assay: Tm pH:3.38 ; Experimental Assay: dHvH pH:3.38 ; Experimental Assay: dHcal pH:3.22 ; Experimental Assay: Tm pH:3.22 ; Experimental Assay: dHvH pH:3.22 ; Experimental Assay: dHcal pH:3.0 ; Experimental Assay: Tm pH:3.0 ; Experimental Assay: dHvH pH:3.0 ; Experimental Assay: dHcal pH:2.85 ; Experimental Assay: Tm pH:2.85 ; Experimental Assay: dHvH pH:2.85 ; Experimental Assay: dHcal pH:3.18 ; Experimental Assay: Tm pH:3.18 ; Experimental Assay: dHvH pH:3.18 ; Experimental Assay: dHcal pH:2.84 ; Experimental Assay: Tm pH:2.84 ; Experimental Assay: dHvH pH:2.84 ; Experimental Assay: dHcal pH:3.25 ; Experimental Assay: Tm pH:3.25 ; Experimental Assay: dHvH pH:3.25 ; Experimental Assay: dHcal pH:3.1 ; Experimental Assay: Tm pH:3.1 ; Experimental Assay: dHvH pH:3.1 ; Experimental Assay: dHcal pH:2.98 ; Experimental Assay: Tm pH:2.98 ; Experimental Assay: dHvH pH:2.98 ; Experimental Assay: dHcal pH:3.26 ; Experimental Assay: Tm pH:3.26 ; Experimental Assay: dHvH pH:3.26 ; Experimental Assay: dHcal pH:3.02 ; Experimental Assay: Tm pH:3.02 ; Experimental Assay: dHvH pH:3.02 ; Experimental Assay: dHcal pH:2.67 ; Experimental Assay: Tm pH:2.67 ; Experimental Assay: dHvH pH:2.67 ; Experimental Assay: dHcal pH:3.28 ; Experimental Assay: Tm pH:3.28 ; Experimental Assay: dHvH pH:3.28 ; Experimental Assay: dHcal pH:2.61 ; Experimental Assay: Tm pH:2.61 ; Experimental Assay: dHvH pH:2.61 ; Experimental Assay: dHcal pH:3.15 ; Experimental Assay: Tm pH:3.15 ; Experimental Assay: dHvH pH:3.15 ; Experimental Assay: dHcal pH:2.99 ; Experimental Assay: Tm pH:2.99 ; Experimental Assay: dHvH pH:2.99 ; Experimental Assay: dHcal pH:2.88 ; Experimental Assay: Tm pH:2.88 ; Experimental Assay: dHvH pH:2.88 ; Experimental Assay: dHcal pH:2.82 ; Experimental Assay: Tm pH:2.82 ; Experimental Assay: dHvH pH:2.82 ; Experimental Assay: dHcal pH:2.6 ; Experimental Assay: Tm pH:2.6 ; Experimental Assay: dHvH pH:2.6 ; Experimental Assay: dHcal pH:3.3 ; Experimental Assay: Tm pH:3.3 ; Experimental Assay: dHvH pH:3.3 ; Experimental Assay: dHcal pH:3.14 ; Experimental Assay: Tm pH:3.14 ; Experimental Assay: dHvH pH:3.14 ; Experimental Assay: dHcal pH:3.01 ; Experimental Assay: Tm pH:3.01 ; Experimental Assay: dHvH pH:3.01 ; Experimental Assay: dHcal pH:2.96 ; Experimental Assay: Tm pH:2.96 ; Experimental Assay: dHvH pH:2.96 ; Experimental Assay: dHcal pH:2.66 ; Experimental Assay: Tm pH:2.66 ; Experimental Assay: dHvH pH:2.66 ; Experimental Assay: dHcal pH:3.21 ; Experimental Assay: Tm pH:3.21 ; Experimental Assay: dHvH pH:3.21 ; Experimental Assay: dHcal pH:3.2 ; Experimental Assay: Tm pH:3.2 ; Experimental Assay: dHvH pH:3.2 ; Experimental Assay: dHcal pH:2.91 ; Experimental Assay: Tm pH:2.91 ; Experimental Assay: dHvH pH:2.91 ; Experimental Assay: dHcal pH:3.45 ; Experimental Assay: Tm pH:3.45 ; Experimental Assay: dHvH pH:3.45 ; Experimental Assay: dHcal pH:3.24 ; Experimental Assay: Tm pH:3.24 ; Experimental Assay: dHvH pH:3.24 ; Experimental Assay: dHcal pH:3.09 ; Experimental Assay: Tm pH:3.09 ; Experimental Assay: dHvH pH:3.09 ; Experimental Assay: dHcal pH:2.83 ; Experimental Assay: Tm pH:2.83 ; Experimental Assay: dHvH pH:2.83 ; Experimental Assay: dHcal pH:2.65 ; Experimental Assay: Tm pH:2.65 ; Experimental Assay: dHvH pH:2.65
Libraries Mutations for sequence KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Lysozyme C P79179 LYSC_GORGO
100.0 Lysozyme C P61626 LYSC_HUMAN
100.0 Lysozyme C P61627 LYSC_PANPA
100.0 Lysozyme C P61628 LYSC_PANTR
99.2 Lysozyme C P79239 LYSC_PONPY
96.9 Lysozyme C P79180 LYSC_HYLLA