Mapping long-range contacts in a highly unfolded protein.
Mapping long-range contacts in a highly unfolded protein.
复制标题
绘制高度未折叠蛋白质中的长程接触图。
DOI：
10.1016/s0022-2836(02)00847-1
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发表时间：
2002
影响因子：
5.6
通讯作者：
Wright,PeterE
中科院分区：
文献类型：
--
作者：
Lietzow,MichaelA;Jamin,Marc;Dyson,HJane;Wright,PeterE
通过分析未折叠或部分折叠状态的构象倾向，可以深入了解蛋白质折叠的最早事件。已使用顺磁自旋标记和 NMR 表征了脱辅基肌红蛋白的酸解折叠状态的结构。通过与位置 18、77 和 133 处的突变半胱氨酸残基偶联而引入的氮氧侧链被用作链压缩和长程三级接触的探针。在 N 端和 C 端之间观察到显着的相互作用，而多肽链的中心区域表现为随机聚合物。即使在这种高度变性的形式下，蛋白质样品也会呈现短暂的紧凑状态，其中 N 端和 C 端区域之间存在类似天然的接触。
Insights into the earliest events in protein folding can be obtained by analysis of the conformational propensities of unfolded or partly folded states. The structure of the acid-unfolded state of apomyoglobin has been characterized using paramagnetic spin labeling and NMR. Nitroxide side-chains, introduced by coupling to mutant cysteine residues at positions 18, 77, and 133, were used as probes of chain compaction and long-range tertiary contacts. Significant interactions are observed within and between the N and C termini, while the central region of the polypeptide chain behaves as a random polymer. Even in this highly denatured form, the protein samples transient compact states in which there are native-like contacts between the N and C-terminal regions.