کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1206099 | 1493707 | 2008 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Probing protein surface accessibility of amino acid substitutions using hydrophobic interaction chromatography
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Probing protein surface accessibility of amino acid substitutions using hydrophobic interaction chromatography Probing protein surface accessibility of amino acid substitutions using hydrophobic interaction chromatography](/preview/png/1206099.png)
چکیده انگلیسی
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 (R2 > 0.85), which clearly indicate that the results can be used for protein retention prediction as well as probing surface properties of protein variants.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Chromatography A - Volume 1215, Issues 1–2, 26 December 2008, Pages 152–155
Journal: Journal of Chromatography A - Volume 1215, Issues 1–2, 26 December 2008, Pages 152–155
نویسندگان
Kristian Becker, Marie Grey, Leif Bülow,