کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10755629 | 1050376 | 2014 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Insights into structural features determining odorant affinities to honey bee odorant binding protein 14
ترجمه فارسی عنوان
نگاهی به ویژگی های ساختاری نشان می دهد که وابستگی های تنفسی به پروتئین متصل به زنبور عسل 14
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
Molecular interactions between odorants and odorant binding proteins (OBPs) are of major importance for understanding the principles of selectivity of OBPs towards the wide range of semiochemicals. It is largely unknown on a structural basis, how an OBP binds and discriminates between odorant molecules. Here we examine this aspect in greater detail by comparing the C-minus OBP14 of the honey bee (Apis mellifera L.) to a mutant form of the protein that comprises the third disulfide bond lacking in C-minus OBPs. Affinities of structurally analogous odorants featuring an aromatic phenol group with different side chains were assessed based on changes of the thermal stability of the protein upon odorant binding monitored by circular dichroism spectroscopy. Our results indicate a tendency that odorants show higher affinity to the wild-type OBP suggesting that the introduced rigidity in the mutant protein has a negative effect on odorant binding. Furthermore, we show that OBP14 stability is very sensitive to the position and type of functional groups in the odorant.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 1042-1046
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 1042-1046
نویسندگان
Andreas Schwaighofer, Maria Pechlaner, Chris Oostenbrink, Caroline Kotlowski, Can Araman, Rosa Mastrogiacomo, Paolo Pelosi, Wolfgang Knoll, Christoph Nowak, Melanie Larisika,