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首页> 美国卫生研究院文献>Protein Science : A Publication of the Protein Society >Analysis of the internal motion of free and ligand-bound human lysozyme by use of 15N NMR relaxation measurement: a comparison with those of hen lysozyme.
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Analysis of the internal motion of free and ligand-bound human lysozyme by use of 15N NMR relaxation measurement: a comparison with those of hen lysozyme.

机译：使用15N NMR弛豫测量分析游离的和配体结合的人溶菌酶的内部运动：与鸡溶菌酶的比较。

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摘要

Human lysozyme has a structure similar to that of hen lysozyme and differs in amino acid sequence by 51 out of 129 residues with one insertion at the position between 47 and 48 in hen lysozyme. The backbone dynamics of free or (NAG)3-bound human lysozyme has been determined by measurements of 15N nuclear relaxation. The relaxation data were analyzed using the Lipari-Szabo formalism and were compared with those of hen lysozyme, which was already reported (Mine S et al.. 1999, J Mol Biol 286:1547-1565). In this paper, it was found that the backbone dynamics of free human and hen lysozymes showed very similar behavior except for some residues, indicating that the difference in amino acid sequence did not affect the behavior of entire backbone dynamics, but the folded pattern was the major determinant of the internal motion of lysozymes. On the other hand, it was also found that the number of residues in (NAG)3-bound human and hen lysozymes showed an increase or decrease in the order parameters at or near active sites on the binding of (NAG)3, indicating the increase in picosecond to nanosecond. These results suggested that the immobilization of residues upon binding (NAG)3 resulted in an entropy penalty and that this penalty was compensated by mobilizing other residues. However, compared with the internal motions between both ligand-bound human and hen lysozymes, differences in dynamic behavior between them were found at substrate binding sites, reflecting a subtle difference in the substrate-binding mode or efficiency of activity between them.
机译：人溶菌酶具有与鸡溶菌酶相似的结构，并且在129个残基中有51个氨基酸序列不同，其中一个插入在鸡溶菌酶的47至48之间。游离或（NAG）3结合的人类溶菌酶的主链动力学已通过测量15 N核弛豫来确定。使用Lipari-Szabo形式主义分析弛豫数据，并将其与已经报道过的鸡溶菌酶的溶酶数据进行比较（Mine S等人，1999，J Mol Biol 286：1547-1565）。在本文中，发现游离的人和鸡溶菌酶的主链动力学表现出非常相似的行为，除了一些残基，这表明氨基酸序列的差异不会影响整个主链动力学的行为，但折叠模式是溶菌酶内部运动的主要决定因素。另一方面，还发现（NAG）3结合的人和母鸡溶菌酶中的残基数量在（NAG）3结合的活性位点处或附近显示顺序参数的增加或减少，表明从皮秒增加到纳秒这些结果表明，结合时残基的固定化（NAG）3导致熵损失，而该损失可通过动员其他残基来补偿。但是，与配体结合的人和母鸡溶菌酶之间的内部运动相比，在底物结合位点发现了它们之间动态行为的差异，这反映了底物结合方式或活性效率之间的细微差异。

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