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The effect of process conditions on the co-processing technology of crude oil and coal was investigated. Crude oil/coal matching performance, swelling degree, crude oil/coal slurry viscosity-temperature characteristics and process parameters were obtained via the laboratory scale and pilot scale studies. The optimum reaction temperature of the co-processing was 445~450 oC, the pressure was 19 MPa, the catalyst addition was 3 wt.%, the reaction time was 2 h, and the ratio of hydrogen to crude oil was 1500 (V/V). Furthermore, the co-processing technology including catalyst and corresponding equipment based on the slurry bed hydrogenation were developed. By using this co-processing technology, the feed ratio of crude oil and coal can be 1:1, the coal conversion rate can be over 99%, the light oil (oil and aromatics) yield was over 70%, and the end products were gasoline, diesel, jet fuel, aromatics and LPG. The product quality meets the Euro V standard, whilst aromatics accounted for 48% of the light oil. So it was proved to be feasible to co-refine crude oil and coal at a ratio of 1:1. What’s more, the slurry bed hydrogenation plant and its equipment were tested for long-term operation, and it has been proved that this co-processing technology could be deployed as large-scale industrial application.

It is generally believed that a protein’s sequence uniquely determines its structure, the basis for a protein to perform biological functions. However, as a representative metamorphic protein, RfaH can be encoded by a single amino acid sequence into two distinct native state structures. Its C-terminal domain (CTD) either takes an all-α-helical configuration to pack tightly with its N-terminal domain (NTD), or the CTD disassociates from the NTD, transforms into an all-β-barrel fold, and further attaches to the ribosome, leaving the NTD exposed to bind RNA polymerases. Therefore, the RfaH protein couples transcription and translation processes. Although previous studies have provided a preliminary understanding of its function, the full course of the conformational change of RfaH-CTD at the atomic level is elusive. We used teDA2, a feature space-based enhanced sampling protocol, to explore the transformation of RfaH-CTD. We found that it undergoes a large-scale structural rearrangement, with characteristic spectra as the fingerprint, and a global unfolding transition with a tighter and energetically moderate molten globule-like nucleus formed in between. The formation of this nucleus limits the possible intermediate conformations, facilitates the formation of secondary and tertiary structures, and thus ensures the efficiency of transformation. The key features along the transition path disclosed from this work are likely associated with the evolution of RfaH, such that encoding a single sequence into multiple folds with distinct biological functions is energetically unhindered.