caa a22 4500 378916157 CHVBK 20180305123553.0 cr unu---uuuuu 161128e20040105xx s 000 0 eng 10.1515/BC.2004.012 doi (NATIONALLICENCE)gruyter-10.1515/BC.2004.012 In vitro folding and characterization of the p53 DNA binding domain [Elektronische Daten] [C. Klein, F. Hesse, A. Dehner, R. A. Engh, M. Schwaiger, S. Hansen] The transcription factor p53 acts as major tumor suppressor and is inactivated by mutation in more than 50% of all human tumors. We have established an efficient procedure for the in vitro folding and purification of the p53 DNA binding domain (p53DBD) using a modified factorial matrix approach that supplies large amounts of homogeneous (isotope-labeled) p53DBD for application in biochemical, crystallographic and NMR spectroscopic studies. We further show with biophysical methods that in vitro folded p53DBD is fully functional and that its conformation is identical to that obtained from the soluble fraction. Copyright © 2004 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Klein C. aut Hesse F. aut Dehner A. aut Engh R. A. aut Schwaiger M. aut Hansen S. aut Biological Chemistry Walter de Gruyter 385/1(2004-01-05), 95-102 1431-6730 385:1<95 2004 385 bchm https://doi.org/10.1515/BC.2004.012 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2004.012 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Klein C. aut NATIONALLICENCE 700 1- Hesse F. aut NATIONALLICENCE 700 1- Dehner A. aut NATIONALLICENCE 700 1- Engh R. A. aut NATIONALLICENCE 700 1- Schwaiger M. aut NATIONALLICENCE 700 1- Hansen S. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 385/1(2004-01-05), 95-102 1431-6730 385:1<95 2004 385 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter