Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment |
Tompa, Peter
(Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences)
Han, Kyou-Hoon (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) Bokor, Monika (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences) Kamasa, Pawel (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences) Tantos, Agnes (Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences) Fritz, Beata (Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences) Kim, Do-Hyoung (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) Lee, Chewook (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) Verebelyi, Tamas (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences) Tompa, Kalman (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences) |
1 | Dunker AK, Obradovic Z, Romero P, Garner EC and Brown CJ (2000) Intrinsic protein disorder in complete genomes. Genome Inform 11, 161-171 |
2 | Lee SH, Kim DH, Han JJ et al (2012) Understanding pre-structured motifs (PreSMos) in intrinsically unfolded proteins. Curr Protein Pept Sci 13, 34-54 DOI |
3 | Dunker AK, Lawson JD, Brown CJ et al (2001) Intrinsically disordered protein. J Mol Graph Model 19, 26-59 DOI |
4 | Uversky VN, Olefiled CJ and Dunker AK (2008) Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu Rev Biophys 37, 215-246 DOI |
5 | Obradovic Z, Peng K, Vucetic S, Radivojac P and Dunker AK (2005) Exploiting heterogeneous sequence properties improves prediction of protein disorder. PROTEINS: Structure, Function, and Bioinformatics Suppl 7, 176-182 DOI |
6 | Bax A and Grzesiek S (1993) Methodological advances in protein NMR. Acc Chem Res 26, 131-138 DOI |
7 | Clore G and Gronenborn A (1991) Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390-1399 DOI |
8 | Hazy E, Bokor M, Kalmar L et al (2011) Distinct hydration properties of wild-type and familial point mutant A53T of alpha-Synuclein associated with Parkinson's disease. Biophys J 101, 2260-2266 DOI |
9 | Lee H, Mok KH, Muhandiram R et al (2000) Local structural elements in the mostly unstructured transcriptional activation domain of human p53. J Biol Chem 275, 29426-29432 DOI |
10 | Fuxreiter M, Simon I, Friedrich P and Tompa P (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 338, 1015-1026 DOI |
11 | Tompa K, Banki P, Bokor M, Kamasa P, Lasanda G and Tompa P (2009) Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions. Biophys J 96, 2789-2798 DOI |
12 | Tompa K, Bokor M and Tompa P (2012) Wide-line NMR and protein hydration in intrinsically disordered protein analysis. Uversky VN, Dunker AK(eds.),167-196, Humana Press |
13 | Coke R and Kuntz ID (1974) The properties of water in biological systems. Annu Rev Biophys Bioeng 3, 95-126 DOI |
14 | Tompa K, Bokor M and Tompa P (2010) Hydration of intrinsically disordered proteins from wide-line NMR : In instrumental analysis of intrinsically disordered proteins: assessing structure and conformation. Uversky VN, Longhi S (eds.), 345-368, John Wiley & Sons Inc |
15 | Kamasa P, Bokor M, Pyda M and Tompa K (2007) DSC approach for the investigation of mobile water fractions in aqueous solutions of NaCl and Tris buffer. Thermochimica Acta 464, 29-34 DOI |
16 | Tompa K, Banki P, Bokor M, Kamasa P, Lasanda G and Tompa P (2009) Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions. Biophys J 96, 2789-2798 DOI |
17 | Tompa K, Bokor M, Verebélyi T and Tompa P (2015) Rotation barriers on protein molecular surfaces. Chem Phys 448, 15-25 DOI |
18 | Tompa P, Banki P, Bokor M et al (2006) Protein-water and protein- buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 91, 2243-2249 DOI |
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