蛋白质折叠动力学对表面疏水取代的稳健性。
Robustness of protein folding kinetics to surface hydrophobic substitutions.
作者信息
Gu H, Doshi N, Kim D E, Simons K T, Santiago J V, Nauli S, Baker D
机构信息
Department of Biochemistry, University of Washington, Seattle 98195, USA.
出版信息
Protein Sci. 1999 Dec;8(12):2734-41. doi: 10.1110/ps.8.12.2734.
Abstract
We use both combinatorial and site-directed mutagenesis to explore the consequences of surface hydrophobic substitutions for the folding of two small single domain proteins, the src SH3 domain, and the IgG binding domain of Peptostreptococcal protein L. We find that in almost every case, destabilizing surface hydrophobic substitutions have much larger effects on the rate of unfolding than on the rate of folding, suggesting that nonnative hydrophobic interactions do not significantly interfere with the rate of core assembly.
摘要
我们使用组合诱变和定点诱变技术来探究表面疏水取代对两种小单结构域蛋白（即原癌基因酪氨酸蛋白激酶Src的SH3结构域和消化链球菌属蛋白L的IgG结合结构域）折叠的影响。我们发现，几乎在每种情况下，使蛋白不稳定的表面疏水取代对去折叠速率的影响远大于对折叠速率的影响，这表明非天然疏水相互作用不会显著干扰核心组装速率。
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本文引用的文献
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The sequences of small proteins are not extensively optimized for rapid folding by natural selection.小蛋白质的序列并未通过自然选择得到广泛优化以实现快速折叠。
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