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首页> 外文期刊>Biochemistry >A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.
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A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.

机译：牛胰胰蛋白酶抑制剂自缔合的脉冲场梯度NMR研究。

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Previous studies have produced conflicting interpretations regarding the aggregation state of BPTI in solution. Here, pulsed-field gradient NMR self-association measurements have been performed with BPTI under a variety of temperature, pH, salt, urea conditions, and protein concentrations. Relative to the standard proteins, lysozyme, ribonuclease, and ubiquitin, diffusion constants indicate that BPTI dimerizes at concentrations above about 3 mg/mL and below 280 K. At higher temperatures, a marked self-association is observed above 10 mg/mL. The apparent lack of significant effects from variations in pH and NaCl concentration suggests minimal contribution to the aggregation process from charge-charge interactions. In contrast, in nondenaturing concentrations of urea (2 M), BPTI behaves as a monomer, suggesting that hydrophobic and polar residues modulate BPTI association. The BPTI surface shows that while one side is highly charged, the opposite side, composed mostly of hydrophobic and some hydrophilic residues, is feasible as an interface for BPTI self-association.
机译：先前的研究对溶液中BPTI的聚集状态产生了矛盾的解释。在这里，已经在各种温度，pH，盐，尿素条件和蛋白质浓度下，使用BPTI进行了脉冲场梯度NMR自缔合测量。相对于标准蛋白，溶菌酶，核糖核酸酶和泛素，扩散常数表明BPTI在高于约3 mg / mL和低于280 K的浓度下会二聚。在更高的温度下，观察到明显的自缔合，高于10 mg / mL。 pH和NaCl浓度变化明显缺乏明显影响，表明电荷与电荷相互作用对聚集过程的贡献很小。相反，在尿素（2 M）的非变性浓度下，BPTI表现为单体，表明疏水残基和极性残基可调节BPTI缔合。 BPTI表面显示，尽管一侧带高电，但另一侧（主要由疏水性残基和一些亲水性残基组成）可作为BPTI自缔合的界面。

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