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首页> 外文期刊>Biochemistry >Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
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Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.

机译：蛋氨酸和丙氨酸取代表明，在T4溶菌酶的羧基末端结构域中形成野生型结构是折叠中的限速步骤。

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摘要

In an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine. Methionine, which approximated the size of the original side chain but which is of different shape and flexibility, was also substituted at most of the same sites. Mutations that substantially destabilize the protein and are located in the carboxy-terminal domain generally slow the rate of folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little effect on stability tend to have little effect on the rate, no matter where they are located. These results suggest that, at the rate-limiting step, elements of structure in the C-terminal domain are formed and have a structure similar to that of the fully folded protein. Consistent with this, two variants that somewhat increase the rate of folding (Phe104 --> Met and Val149 --> Met) are located within the carboxy-terminal domain and maintain or improve packing with very little perturbation of the wild-type structure.
机译：为了确定蛋白质结构与其折叠动力学之间的系统关系，我们确定了20种T4溶菌酶突变体的折叠速率，其中有一个庞大的，埋藏的，非极性的野生型残基（Leu，Ile，Phe， Val（或Met）被丙氨酸取代。蛋氨酸近似于原始侧链的大小，但具有不同的形状和柔韧性，在大多数相同的位置也被取代。基本上破坏蛋白质稳定性并位于羧基末端结构域的突变通常会减慢折叠速度。但是，氨基末端结构域中不稳定的突变对折叠速率的影响很小。对稳定性影响很小的突变，无论位于何处，都对速率没有太大影响。这些结果表明，在限速步骤中，形成了C-末端结构域中的结构元件，并具有与完全折叠的蛋白质相似的结构。与此相一致，在羧基末端结构域内存在两个可以稍微提高折叠速率的变体（Phe104-> Met和Val149-> Met），它们可以维持或改善包装，而对野生型结构的干扰很小。

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