![]() At low pH, L99A T4 lysozyme expanded from a compact folded state to a partially unfolded state with a corresponding change in radius of gyration from 17 to 32 Å. To investigate water penetration and the volume change associated with pressure denaturation, we studied the solution behavior of four T4 lysozyme mutants having different cavity volumes at low and neutral pH up to a pressure of 400 MPa (0.1 MPa = 0.9869 atm). Recent studies imply that the mechanism of pressure denaturation is the penetration of water into the protein rather than the transfer of hydrophobic residues into water. the supporting platforms (only if specific).Using small angle X-ray scattering (SAXS) and tryptophan fluorescence spectroscopy, we have identified multiple compact denatured states of a series of T4 lysozyme mutants that are stabilized by high pressures. The haxe externs are attributed with following metadata: To (re)generate for another electron version download the description file from and run: haxe -macro ElectronAPI.generate("optional/path/to/electron-api.json")īuild haxedoc.xml to insure everything is fine: haxe haxedoc.hxmlīy default hxelectron/electron-api.json is used if you ommit the path argument to your custom description file. Haxe type definitions for electron, a framework for building cross-platform desktop applications with JavaScript, HTML, and CSS.ĭevelopment version haxelib git electron Īll type definitions are generated from electron-api.json by ElectronAPI.hx.
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