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首页> 外文期刊>Biochemistry >Hierarchical Folding of Intestinal Fatty Acid Binding Protein
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Hierarchical Folding of Intestinal Fatty Acid Binding Protein

机译：肠道脂肪酸结合蛋白的层次折叠

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摘要

Intestinal fatty acid binding protein (IFABP) is a member of the lipid binding protein family, members of whichhave a clamshell type of motif formed by two five-stranded #beta#-sheets. Understanding the folding mechanism of these proteins has beenhindered by the presence of an unresolved burst phase. By initiating the reactionwith a sub-millisecond mixer and following its progressionby Trp fluorescenc, we discovered three distinct phases in the folding reactionof the W6Y mutant of IFABP from which we postulate the following sequence of events. The first phase (k_1 > 10 000 s~(-1)) involves collapse of the polypeptide chain around a hydrophobic core. During the second phase (k_2 approx 1500 s~(-1)), #beta#-strands B-G, mostly located on the top half of the clam shell structure, propagate from this hydrophobic core. it is followed by the final phase (k_3 approx 5 s~(-1)) involving the formation of the last three #beta#-strands on the bottom half of the clam shell and the establishment of the native hydrogen bonding network throughout the protein molecule.
机译：肠脂肪酸结合蛋白（IFABP）是脂质结合蛋白家族的成员，其成员具有由两个五链＃beta＃-片形成的翻盖型基序。这些蛋白质折叠机制的理解因未解决的猝发相的存在而受阻。通过用亚毫秒混合器启动反应并通过Trp荧光进行反应，我们发现IFABP W6Y突变体折叠反应的三个不同阶段，我们从中推测出以下事件序列。第一阶段（k_1> 10000 s〜（-1））涉及多肽链在疏水核心周围的折叠。在第二阶段（k_2约1500 s〜（-1）），＃beta＃链B-G主要位于蛤壳结构的上半部，从该疏水核扩散。随后是最终阶段（k_3约5 s〜（-1）），该阶段涉及在蛤壳底部的最后三个＃beta＃链的形成以及整个蛋白质中天然氢键网络的建立分子。

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