Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Green fluorescent protein as a reporter of prion protein folding | Virology Journal BioMed Central Research Green fluorescent protein as a reporter of prion protein folding Snezana Vasiljevid Junyuan Rent YongXiu Yao Kevin Dalton Catherine S Adamson and Ian M Jones Open Access Address School of Animal and Microbial Sciences The University of Reading Reading RG6 6AJ UK Email Snezana Vasiljevic - Junyuan Ren - YongXiu Yao - Kevin Dalton - kevindaltoncpfc@ Catherine S Adamson - cadamson@ Ian M Jones - Corresponding author fEqual contributors Published 29 August 2006 Received 28 June 2006 Accepted 29 August 2006 Virologyjournal 2006 3 59 doi 186 1743-422X-3-59 This article is available from http content 3 1 59 2006 Vasiljevic et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract_ Background The amino terminal half of the cellular prion protein PrPc is implicated in both the binding of copper ions and the conformational changes that lead to disease but has no defined structure. However as some structure is likely to exist we have investigated the use of an established protein refolding technology fusion to green fluorescence protein GFP as a method to examine the refolding of the amino terminal domain of mouse prion protein. Results Fusion proteins of PrPc and GFP were expressed at high level in and could be purified to near homogeneity as insoluble inclusion bodies. Following denaturation proteins were diluted into a refolding buffer whereupon GFP fluorescence recovered with time. Using several truncations of PrPc the rate of refolding was shown to depend on the prion .
