Publication: Bovine Albuminin Sulu Çözeltisinde 16 Doxyl Steraic Acid ve Tempo Radikallerinin Spin-Etiketleme Tekniği Kullanılarak Epr ile İncelenmesi
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III ÖZET Bu çalışmada, bovine albumin proteini 0.1 M sodyum fosfat çözeltisinde 16 doxyl stearic acid, Tempo, Tempo I, Tempo II radikalleri ile etiketlendi. Bu etiketlerin hareketi 10~10 - 10~7 dönme ilgi zamanları aralığında incelendi. Farklı sıcaklıklarda her bir etiketin dönme ilgi zamanları ve akt;«/asyon enerjileri hesaplandı. Bu incelemelerden bovin albüminin yüzeyindeki SH grubunun çevresinin bir yarık olduğu fikri teyit edildi. Bu çalışmada, biomoleküllerin hidrodinamik yarıçaplarını belirlemede oldukça güçlü teknik olan spin etiketleme tekniği ve EPR spektroskopisi kullanılmıştır. Aynı çalışmada, biomoleküllerdeki su - protein fazının değişik katmanlarının hareketliliği de incelendi.
IV ABSTRACT In this work, bovine albumin protein was labeled with 16 doxyl stearic acid, Tempo, Tempo I, Tempo II radicals in 0.1 M sodium phosphate solution, in order to investigate the motion of labeled protein in the rotational correlation times range 10'10 - 10'7 s with EPR spectroscopy. The rotational correlation times and activation energy of each radical were calculated at different temperatures. In this study, it was indicated that environment of SH group on the surface of bovine albumin is a crevice. It is found that Electron Paramagnetic Resonance Spectroscopy and spin labeling are a very powerful technique in the determination of hydrodynamic radii of biomolecules compared to other techniques. In the same work, the mobility of various layers of water - protein matrix was also investigated.
IV ABSTRACT In this work, bovine albumin protein was labeled with 16 doxyl stearic acid, Tempo, Tempo I, Tempo II radicals in 0.1 M sodium phosphate solution, in order to investigate the motion of labeled protein in the rotational correlation times range 10'10 - 10'7 s with EPR spectroscopy. The rotational correlation times and activation energy of each radical were calculated at different temperatures. In this study, it was indicated that environment of SH group on the surface of bovine albumin is a crevice. It is found that Electron Paramagnetic Resonance Spectroscopy and spin labeling are a very powerful technique in the determination of hydrodynamic radii of biomolecules compared to other techniques. In the same work, the mobility of various layers of water - protein matrix was also investigated.
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Tez (yüksek lisans) -- Ondokuz Mayıs Üniversitesi, 1995
Libra Kayıt No: 37196
Libra Kayıt No: 37196
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64
