In vitro folding and characterization of the p53 DNA binding domain

Verfasser / Beitragende:
[C. Klein, F. Hesse, A. Dehner, R. A. Engh, M. Schwaiger, S. Hansen]
Ort, Verlag, Jahr:
2004
Enthalten in:
Biological Chemistry, 385/1(2004-01-05), 95-102
Format:
Artikel (online)
ID: 378916157
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245 0 0 |a In vitro folding and characterization of the p53 DNA binding domain  |h [Elektronische Daten]  |c [C. Klein, F. Hesse, A. Dehner, R. A. Engh, M. Schwaiger, S. Hansen] 
520 3 |a 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. 
540 |a Copyright © 2004 by Walter de Gruyter GmbH & Co. KG 
690 7 |a Biochemistry  |2 nationallicence 
690 7 |a Molecular biology  |2 nationallicence 
690 7 |a Cellular biology  |2 nationallicence 
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700 1 |a Hesse  |D F.  |4 aut 
700 1 |a Dehner  |D A.  |4 aut 
700 1 |a Engh  |D R. A.  |4 aut 
700 1 |a Schwaiger  |D M.  |4 aut 
700 1 |a Hansen  |D S.  |4 aut 
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