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首页> 外文期刊>Biochemistry >Examination of the Slow Unfolding of Pro-Nerve Growth Factor Argues against a Loop Threading Mechanism for Nerve Growth Factor
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Examination of the Slow Unfolding of Pro-Nerve Growth Factor Argues against a Loop Threading Mechanism for Nerve Growth Factor

机译：前神经生长因子缓慢展开的争论反对神经生长因子的循环穿线机制

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摘要

Nerve growth factor (NGF),a member of the neurotrophin family,is an all-beta-sheet protein with a characteristic structure motif,the cystine knot.Unfolding of NGF in 6 M GdnHCl has been described previously to involve an initial partial loss of structure and a subsequent very slow conversion to a second,completely unfolded state.This latter conversion was postulated to represent a back-threading of the disulfide bond that passes through the cystine knot (loop threading hypothesis).Here,this hypothesis was questioned with the pro form of the protein (proNGF).In proNGF,the mature part is preceded by the 103-amino acid pro-peptide.Consequently,loop threading of the N-terminally extended protein should be significantly delayed.However,unfolding kinetics of proNGF monitored by RP-HPLC,intrinsic fluorescence,and NMR spectroscopy were comparable to those of mature NGF.Time-resolved ~1H- ~(15)N HSQC spectra revealed a slow time-dependent loss of residual structure of which the kinetics correlated well with the transition observed by RP-HPLC.Refolding from the completely unfolded state led to a partial recovery of natively folded proNGF.In summary,the sequential unfolding of proNGF only marginally differed from that of mature NGF.Therefore,it is very unlikely that a loop threading mechanism is the cause of the slow unfolding step.
机译：神经生长因子（NGF）是神经营养蛋白家族的成员，是一种具有特征性结构基序的全β-折叠蛋白，胱氨酸结。6MGdnHCl中NGF的折叠先前已被描述为最初的部分丢失。结构并随后非常缓慢地转换为第二个完全展开的状态。该后一种转换被认为代表了穿过胱氨酸结的二硫键的反螺纹（环螺纹假设）。蛋白质的前体形式（proNGF）。在proNGF中，成熟部分之前是103个氨基酸的前肽。因此，应显着延迟N末端延伸的蛋白质的环穿线。 RP-HPLC，本征荧光和NMR光谱与成熟的NGF相当从RP-HPLC观察到的转变非常好。从完全展开的状态重新折叠导致天然折叠的proNGF的部分恢复。总而言之，proNGF的顺序展开仅与成熟的NGF略有不同，因此，这不太可能循环线程机制是缓慢展开步骤的原因。

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