Direct Observation of Insulin Association Dynamics with Time-Resolved X-ray Scattering.

Direct Observation of Insulin Association Dynamics with Time-Resolved X-ray Scattering.
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DOI:
10.1021/acs.jpclett.7b01720
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发表时间:
2017-09-21
期刊:
The journal of physical chemistry letters
影响因子:
--
通讯作者:
Chen LX
Chen LX
中科院分区:
其他
文献类型:
--
作者:
Rimmerman D;Leshchev D;Hsu DJ;Hong J;Kosheleva I;Chen LX

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Biological functions frequently require protein–protein interactions that involve secondary and tertiary structural perturbation. Here we study protein–protein dissociation and reassociation dynamics in insulin, a model system for protein oligomerization. Insulin dimer dissociation into monomers was induced by a nanosecond temperature-jump (T-jump) of ~8 °C in aqueous solution, and the resulting protein and solvent dynamics were tracked by time-resolved X-ray solution scattering (TRXSS) on time scales of 10 ns to 100 ms. The protein scattering signals revealed the formation of five distinguishable transient species during the association process that deviate from simple two-state kinetics. Our results show that the combination of T-jump pump coupled to TRXSS probe allows for direct tracking of structural dynamics in nonphotoactive proteins.
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