Protein folding: Looping from hydrophobic nuclei
Protein folding: Looping from hydrophobic nuclei
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DOI：
10.1002/prot.1155
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发表时间：
2001-12-01
期刊：
影响因子：
--
通讯作者：
Trifonov, EN
中科院分区：
文献类型：
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作者：
Berezovsky, IN;Kirzhner, VM;Trifonov, EN
蛋白质结构可以被看作是一个紧凑的线性阵列，由25-30个氨基酸残基组成的接近标准尺寸的闭环（Berezovsky et al., FEBS Letters 2000; 466: 283-286），而不考虑二级结构的细节。环路中的端到端接触可能是疏水的，这是一个可验证的假设。这个概念可以通过与Kyte和Doolittle亲水性图的直接比较来验证。这一分析表明，大多数环的末端确实是疏水的。通过对23个全测序细菌基因组蛋白序列的位置自相关分析，得出了相同的结论。疏水残基缬氨酸、丙氨酸、甘氨酸、亮氨酸和异亮氨酸优先出现在彼此之间25-30个残基之间。这些观察结果为理解蛋白质结构和折叠开辟了一个新的视角：多肽链的连续环主要在疏水核处结束。(C) 2001 Wiley-Liss, Inc。
Protein structure can be viewed as a compact linear array of nearly standard size closed loops of 25-30 amino acid residues (Berezovsky et al., FEBS Letters 2000; 466: 283-286) irrespective of details of secondary structure. The end-to-end contacts in the loops are likely to be hydrophobic, which is a testable hypothesis. This notion could be verified by direct comparison of the loop maps with Kyte and Doolittle hydropathicity plots. This analysis reveals that most of the ends of the loops are hydrophobic, indeed. The same conclusion is reached on the basis of positional autocorrelation analysis of protein sequences of 23 fully sequenced bacterial genomes. Hydrophobic residues valine, alanine, glycine, leucine, and isoleucine appear preferentially at the 25-30 residues distance one from another. These observations open a new perspective in the understanding of protein structure and folding: a consecutive looping of the polypeptide chain with the loops ending primarily at hydrophobic nuclei. (C) 2001 Wiley-Liss, Inc.