The speed limit for protein folding measured by triplet-triplet energy transfer
The speed limit for protein folding measured by triplet-triplet energy transfer
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DOI：
10.1073/pnas.96.17.9597
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发表时间：
1999-08-17
影响因子：
11.1
通讯作者：
Kiefhaber, T
中科院分区：
文献类型：
--
作者：
Bieri, O;Wirz, J;Kiefhaber, T
分子内链扩散的直接测量是通过测定多肽链上限定点上连接的供体和受体生色团之间的三重-三重能量转移速率来获得的。供体和受体通过重复的甘氨酸和丝氨酸残基连接在一起的多肽在纳秒时间尺度上观察到接触形成的单指数动力学。这一速率取决于分离供体和受体的多肽键的数目(N)，最短的多肽(N=3)具有最大值，时间常数(tau=ilk)为20 ns。这为蛋白质折叠过程中第一个侧链接触的形成速度设定了上限。
A direct measure of intramolecular chain diffusion is obtained by the determination of triplet-triplet energy-transfer rates between a donor and an acceptor chromophore attached at defined points on a polypeptide chain. Single exponential kinetics of contact formation are observed on the nanosecond time scale for polypeptides in which donor and acceptor are linked by repeating units of glycine and serine residues. The rates depend on the number of peptide bonds (N) separating donor and acceptor and show a maximum for the shortest peptides (N = 3) with a time constant (tau = Ilk) of 20 ns. This sets an upper limit for the speed of formation of the first side-chain contacts during protein folding.