To test whether interactions in the hydrophobic core of a protein can be adequately modeled based on the properties of a liquid hydrocarbon, we measured the unfolding free energies of the wild-type bacteriophage f1 gene V protein and 29 mutants with apolar substitutions at positions 35 and 47. Stability changes arising from identical mutations at these two buried sites are quite different, suggesting that one site is more rigid than the other. Reversals of residues at positions 35 and 47 confirm that their environments are distinct. Mutants containing weakly polar residues at these two sites suggest that the protein interior is more polar than a liquid hydrocarbon. Interactions between residues at the two sites appear to be minimal. These observations are compatible with a view of protein interiors that incorporates properties of liquid hydrocarbons but also includes polar interactions and a site-dependent "packing energy" associated with changes in internal structure. Study holds ProTherm entries: 850, 851, 852, 853, 854, 855, 856, 857, 858, 859, 860, 861, 862, 863, 864, 865, 866, 867, 868, 869, 870, 871, 872, 873, 874, 875, 876, 877, 878, 879 Extra Details: additive : EDTA(1 mM),dG and ddG values were measured in the presence of 2M GdnHCl gene V protein, protein stability, hydrophobic effect;,protein engineering
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:16 p.m.
|Number of data points||179|
|Proteins||DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P ; DNA-Binding protein G5P|
|Assays/Quantities/Protocols||Experimental Assay: Cm ; Experimental Assay: m ; Experimental Assay: dG_H2O ; Experimental Assay: dG ; Derived Quantity: ddG_H2O ; Derived Quantity: ddG|
|Libraries||Mutations for sequence MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEYPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK|