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首页> 外文会议>EU-Korea Conference on Science and Technology >Proteomic Study of Hydrophobic (Membrane) Proteins and Hydrophobic Protein Complexes
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Proteomic Study of Hydrophobic (Membrane) Proteins and Hydrophobic Protein Complexes

机译：疏水性（膜）蛋白和疏水蛋白复合物的蛋白质组学研究

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Over the past decade, understanding of the structure and function of membraneproteins has advanced significantly as well as how their detailed characterization can be ap-proached experimentally. Detergents have played significant roles in this effort. They serve astools to isolate, solubilize, and manipulate membrane proteins for subsequent biochemical andphysical characterization. Combination of detergents and various separation methods coupledwith mass spectrometry technology e.g. MALDI-TOF/TOF and nano-HPLC-ESI-Q-TOF/MS/MS is now possible to examine the expression of membrane proteins. This study forestablishing separation methods of membrane proteins on two modified gel-electrophoresis(16-BAC and BN-PAGE subsequently with SDS-PAGE) could make it likely that the compo-nents of membranes become increasingly amenable to identification and characterization. Tostudy the structure (complexes) and function of membrane proteins, we must firstpre-fractionate enriched membrane proteins, or isolate and purify membrane complexes. Suchproteins can be solubilized by high-salt solutions or detergents, which have affinity both forhydrophobic groups and for water. Due to a preponderance of binding detergents over hydro-phobic regions, when integral proteins are exposed on aqueous solution, these protein mole-cules are prevented from aggregation and maintained their native conformation. Subsequently,diverse kinds of eletrophoretic analysis combined with mass spectrometry have been appliedwith site specific (tripsin, chymotrypsin, CNBr and Asp-N) enzymes. The final goal is to enablehigh-throughput analysis of ion-channel proteins and major neurotransmitter receptor com-plexes within central nervous system by an electrophoretic method allowing quantification withsubsequent unambiguous protein identification.
机译：在过去十年中，了解膜普选蛋白的结构和功能显着提出，以及他们的详细表征如何在实验上进行AP。洗涤剂在这项工作中发挥了重要作用。它们为易于分离，溶解和操纵膜蛋白的易于用于随后的生物化学和物理性表征。洗涤剂的组合与各种分离方法耦合，大众光谱技术耦合。 MALDI-TOF / TOF和纳米HPLC-ESI-Q-TOF / MS / MS现在可以检查膜蛋白的表达。该研究在两个改性凝胶电泳上的常规膜蛋白的违规分离方法（16-BAC和随后用SDS-PAGE的BN-PAGE）可以使膜的组合物变得越来越敏捷以鉴定和表征。扭曲的结构（复合物）和膜蛋白的功能，我们必须富集 - 分馏富集膜蛋白，或分离和纯化膜配合物。这种蛋白质可以通过高盐溶液或洗涤剂溶解，所述高盐溶液或洗涤剂具有亲和力的过度基团和水。由于在水溶液上暴露于水溶液中的结合洗涤剂的优势，从聚集中防止这些蛋白质摩尔内酯并保持其天然构象。随后，与质谱相结合的不同类型的Eletrophoretic分析已经适用于特异性特异性（Tripsin，Chymotrypsin，CNBR和ASP-N）酶。最终目标是通过电泳方法能够在中枢神经系统中能够在中枢神经系统内进行离子通道蛋白和主要神经递质受体COM-PLEX的高度吞吐量分析，允许定量与序列的明确蛋白质鉴定。

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