具有OB折叠结构的葡萄球菌核酸酶片段显示出在报道的“熔球态”范围内的氢交换保护因子。
A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for "molten globules".
作者信息
Alexandrescu A T, Dames S A, Wiltscheck R
机构信息
Department of Structural Biology, Biozentrum, University of Basel, Switzerland.
出版信息
Protein Sci. 1996 Sep;5(9):1942-6. doi: 10.1002/pro.5560050924.
Abstract
Hydrogen-exchange rates for an OB-fold subdomain fragment of staphylococcal nuclease have been measured at pH 4.7 and 4 degrees C, conditions close to the minimum of acid/base catalyzed exchange. The strongest protection from solvent exchange is observed for residues from a five-stranded beta-barrel in the NMR structure of the protein. Protection factors, calculated from the experimental hydrogen-exchange rates, range between 1 and 190. Similarly small protection factors have in many cases been attributed to "molten globule" conformations that are supposed to lack a specific tertiary structure. The present results suggest that marginal protection from solvent exchange does not exclude well-defined structure.
摘要
已在pH 4.7和4℃条件下测量了葡萄球菌核酸酶一个OB折叠亚结构域片段的氢交换率，该条件接近酸/碱催化交换的最小值。在该蛋白质的NMR结构中，对来自五链β桶的残基观察到最强的溶剂交换保护作用。根据实验氢交换率计算出的保护因子在1到190之间。在许多情况下，类似的小保护因子被归因于假定缺乏特定三级结构的“熔球”构象。目前的结果表明，对溶剂交换的边际保护并不排除明确的结构。
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