1jl2: Difference between revisions

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{{STRUCTURE_1jl2|  PDB=1jl2  |  SCENE=  }}  
{{STRUCTURE_1jl2|  PDB=1jl2  |  SCENE=  }}  


'''Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H'''
===Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H===




==Overview==
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To investigate the contribution of the folding cores to the thermodynamic stability of RNases H, we used rational design to create two chimeras composed of parts of a thermophilic and a mesophilic RNase H. Each chimera combines the folding core from one parent protein and the remaining parts of the other. Both chimeras form active, well-folded RNases H. Stability curves, based on CD-monitored chemical denaturations, show that the chimera with the thermophilic core is more stable, has a higher midpoint of thermal denaturation, and a lower change in heat capacity (DeltaCp) upon unfolding than the chimera with the mesophilic core. A possible explanation for the low DeltaCp of both the parent thermophilic RNase H and the chimera with the thermophilic core is the residual structure in the denatured state. On the basis of the studied parameters, the chimera with the thermophilic core resembles a true thermophilic protein. Our results suggest that the folding core plays an essential role in conferring thermodynamic parameters to RNases H.
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{{ABSTRACT_PUBMED_11790848}}


==About this Structure==
==About this Structure==
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[[Category: Robic, S.]]
[[Category: Robic, S.]]
[[Category: Mixed alpha-beta protein]]
[[Category: Mixed alpha-beta protein]]
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