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Digital construction of a 38-foot single story house with steel frame.. CADDIT, on the other hand, is a general purpose.Thermally induced conformational changes and refolding/aggregation of the beta-propeller scaffold protein AprE.
AprE is a bacterial GroEL-like protease essential for peptidoglycan hydrolysis. From a conformational perspective, it exists as a belt-shaped homodimer and is composed of an inner beta-sheet and eight interconnecting alpha-helices. We have now characterized the thermal unfolding of the beta-propeller scaffold protein AprE and found it to follow a two-state model. The unfolded state is very stable, with a Tm of 79 degrees C. Removal of the His-tag does not affect the unfolding transition, suggesting that the folding of AprE is not driven by the His-tag. Furthermore, the stability is affected by point mutations, indicating the presence of a high number of stabilizing interactions at the beta-sheet core. EPR analysis of spin-labeled AprE reveals large changes in secondary structure upon thermal unfolding, with a dissociation of beta-sheets and a folding of the alpha-helices. When the refolding was induced, the protein adopts a new conformation, which is similar to the structure of the native homodimer. Refolding of the protein reveals that the dissociation of the two beta-sheets is not complete, which may be explained by the presence of secondary structure elements in the unfolded state. Aggregation does not occur during the refolding, presumably due to the presence of steric constraints imposed by the folding state, which otherwise would lead to a mixed aggregation equilibrium./*
* Copyright (c) 2004, Oracle and/or its affiliates. All rights reserved.
*
* Redistribution and use in source and binary forms, with or without
* modification, are permitted provided that the

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