Becker Kristian, Grey Marie, Bülow Leif
Department of Pure and Applied Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-211 00 Lund, Sweden.
J Chromatogr A. 2008 Dec 26;1215(1-2):152-5. doi: 10.1016/j.chroma.2008.11.002. Epub 2008 Nov 7.
Hydrophobic interaction chromatography (HIC) has been used to determine the influence of amino acid substitutions on protein retention and thereby their accessibility on the protein surface. The retentions of mutants of green fluorescent protein (GFPuv) and human hemoglobin (Hb) were studied on multimodal HIC media and compared to the hydrophobicities from known hydrophobicity scales with respect to the accessible surface area. For GFPuv, the theoretical and experimental results of three hydrophobicity scales correlated well (R(2)>0.85), which clearly indicate that the results can be used for protein retention prediction as well as probing surface properties of protein variants.
疏水相互作用色谱法（HIC）已被用于确定氨基酸取代对蛋白质保留的影响，从而确定其在蛋白质表面的可及性。在多模式HIC介质上研究了绿色荧光蛋白（GFPuv）和人血红蛋白（Hb）突变体的保留情况，并将其与已知疏水性标度中关于可及表面积的疏水性进行了比较。对于GFPuv，三种疏水性标度的理论和实验结果相关性良好（R²>0.85），这清楚地表明这些结果可用于蛋白质保留预测以及探测蛋白质变体的表面性质。
