SMALL-ANGLE NEUTRON-SCATTERING STUDY OF THE STRUCTURE OF PROTEIN DETERGENT COMPLEXES

SMALL-ANGLE NEUTRON-SCATTERING STUDY OF THE STRUCTURE OF PROTEIN DETERGENT COMPLEXES
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DOI:
10.1002/bip.360290206
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发表时间:
1990-02-05
期刊:
影响因子:
2.9
通讯作者:
TEIXEIRA, J
TEIXEIRA, J
中科院分区:
生物学4区
文献类型:
--
作者:
GUO, XH;ZHAO, NM;TEIXEIRA, J

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用小角中子散射(SANS)研究了蛋白质/十二烷基硫酸钠复合物的结构。使用两种水溶性蛋白质,牛血清白蛋白(BSA)和卵清蛋白(OVA)。蛋白质浓度保持恒定在1重量%,蛋白质/洗涤剂重量比在1/1、1/1.5、1/2和1/3之间变化。用分形模型分析了SANS分布的绝对强度。SANS分布的大Q部分的分析建立了十二烷基硫酸钠(SDS)分子结合到蛋白质/SDS复合物形成胶束状簇。另一方面,SANS分布的小Q部分的分析清楚地表明,胶束状簇的排列类似于球的分形堆积。我们发现,一个蛋白质/SDS复合物的特征在于从散射实验中提取的四个参数,即,平均胶束的大小和聚集数,表征胶束链的构象的分形维数,相关长度给展开的多肽链的程度,和胶束样簇在复合物中的数量。
Small-angle neutron scattering (SANS) was used to study the structure of protein/sodium dodecylsulfate complexes. Two water soluble proteins, bovine serum albumin (BSA) and ovalbumin (OVA), were used. The protein concentration was kept constant at 1 wt %, and protein/detergent wt ratio varied between 1/1, 1/1.5, 1/2 and 1/3. Absolute intensities of SANS distributions were analyzed by a fractal model. Analyses of large Q portions of SANS distributions established that sodium dodecylsulfate (SDS) molecules bound to a protein/SDS complex form micelle-like clusters. On the other hand, analyses of small Q portions of SANS distributions clearly showed that the arrangement of micelle-like clusters resembles a fractal packing of spheres. We showed that a protein/SDS complex can be characterized by four parameters extracted from the scattering experiment, namely, the average micelle size and its aggregation number, the fractal dimension characterizing the conformation of the micellar chains, the correlation length giving the extent of the unfolded polypeptide chains, and the numbers of micelle-like clusters in the complex.