%0 Journal Article
%T Determination of free energy of protein folding on liquid-solid interface<br>
%A GENG Xindu
%A ZHANG Jing
%A WEI Yinmao
%A <br>
%J 科学通报(英文版)
%D 2000
%I 
%X Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, ΔΔGF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the ΔΔGF is established. Lysozyme and α-amylase have been selected as examples to test the new method, and their ΔΔGF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the ΔΔGF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations, ±4.7% for lysozyme and ±3.0% for α-amylase, indicate that the new method has a satisfactory reproducibility and reliability.
%K stoichiometric displacement model
%K high-performance hydrophobic interaction chromatography
%K adsorption free energy
%K protein folding<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=01BA20E8BA813E1908F3698710BBFEFEE816345F465FEBA5&cid=96E6E851B5104576C2DD9FC1FBCB69EF&jid=DD6615BC9D2CFCE0B6F945E8D5314523&aid=0FB497982177B9D84AB5B308953E2553&yid=9806D0D4EAA9BED3&vid=94E7F66E6C42FA23&iid=38B194292C032A66&sid=FE4C96E058BB2280&eid=6A73B36E85DB0CE9&journal_id=1001-6538&journal_name=科学通报(英文版)&referenced_num=2&reference_num=15