Structural resolution of the folding pathway of a protein by correlation of phi-values with inter-residue contacts.
Structural resolution of the folding pathway of a protein by correlation of phi-values with inter-residue contacts.
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通过 phi 值与残基间接触的相关性来解析蛋白质折叠途径的结构。
DOI：
10.1006/jtbi.1998.0783
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发表时间：
1998
影响因子：
2
通讯作者：
B. Nölting
中科院分区：
文献类型：
--
作者：
B. Nölting
barstar 是核糖核酸酶 barnase 的 10 kD 抑制剂，其折叠被建议遵循成核-缩合模型 [Nölting, B., Golbik, R., Neira, J. L., Soler-Gonzalez, A. S., Schreiber, G. & Fersht, A. R. (1997)。过程。纳特。阿卡德。科学。 U.S.A. 94, 826-830]，其中结构生长从分子的特定区域（折叠核）开始。这里，通过使用与残基间接触图相关的 phi 值来绘制扩散核的结构及其在折叠反应开始后 500 微米、1 毫秒和 100 毫秒三个阶段的生长。 Barstar折叠是通过在微秒时间尺度内strand1-loop1-helix1基序内部和周围相互作用的显着巩固而启动的，随后是helix4的巩固，helix4位于靠近C末端并且在冷变性状态下不具有显着的残余结构。不均匀的结构固结在折叠的早期阶段最为明显。 barstar 的晚期折叠事件的特征是结构整合从 N 端和 C 端向位于序列中心的残基传播。
Folding of barstar, the 10 kDalton inhibitor of the ribonuclease barnase, has been suggested to follow a nucleation-condensation model [Nölting, B., Golbik, R., Neira, J. L., Soler-Gonzalez, A. S., Schreiber, G. & Fersht, A. R. (1997). Proc. Nat. Acad. Sci. U.S.A. 94, 826-830], where structure growth starts in a particular region of the molecule, the folding nucleus. Here the structure of the diffuse nucleus and its growth in three stages, 500 micros, 1 ms and 100 ms after initiation of the folding reaction, is mapped out by using phi-values which are correlate with inter-residue contact plots. Barstar folding is initiated by a significant consolidation of interactions in and around the strand1-loop1-helix1 motif in the microsecond time scale, followed by the consolidation of helix4, which is located close to the C-terminus and does not have significant residual structure in the cold-denatured state. The non-uniform structure consolidation is most pronounced in the early stages of folding. The late folding events of barstar are characterized by a propagation of structure consolidation from the N-and C-termini towards residues located in the center of the sequence.