Planck-Benzinger thermal work function: thermodynamic characterization of the carboxy-terminus of p53 peptide fragments
- PMID: 21086029
- DOI: 10.1007/s10930-010-9286-9
Planck-Benzinger thermal work function: thermodynamic characterization of the carboxy-terminus of p53 peptide fragments
Abstract
The thermodynamic parameters for six p53 carboxy-terminus peptide fragments as determined by analytical ultracentrifugal analysis were compared over the experimental temperature range of 275-310 K to evaluate the Gibbs free energy change as a function of temperature, ΔG°(T), from 0 to 400 K using our general linear third-order fitting function, ΔG°(T) = α + βT² + γT³. Data obtained at the typical experimental temperature range are not sufficient to accurately describe the variations observed in the oligomerization of these p53 fragments. It is necessary to determine a number of thermodynamic parameters, all of which can be precisely assessed using this general third-order linear fitting function. These are the heat of reaction, innate temperature-invariant enthalpy, compensatory temperatures and the thermodynamic molecular switch occurring at the thermal set point. This methodology can be used to distinguish the characteristic structure and stability of p53 carboxy-terminal fragments or other p53 mutants. It should be used for the thermodynamic characterization of any interacting biological system.
Similar articles
-
Molecular-level thermodynamic switch controls chemical equilibrium in sequence-specific hydrophobic interaction of 35 dipeptide pairs.Biophys J. 2003 Feb;84(2 Pt 1):1352-69. doi: 10.1016/S0006-3495(03)74951-0. Biophys J. 2003. PMID: 12547816 Free PMC article.
-
Thermodynamic molecular switch in sequence-specific hydrophobic interaction: two computational models compared.ScientificWorldJournal. 2003 Mar 31;3:176-93. doi: 10.1100/tsw.2003.16. ScientificWorldJournal. 2003. PMID: 12806129 Free PMC article. Review.
-
Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes.Biochemistry. 2003 Feb 25;42(7):2202-17. doi: 10.1021/bi0270992. Biochemistry. 2003. PMID: 12590610
-
Comparison of BRCT domains of BRCA1 and 53BP1: a biophysical analysis.Protein Sci. 2004 Mar;13(3):617-25. doi: 10.1110/ps.03461404. Protein Sci. 2004. PMID: 14978302 Free PMC article.
-
Structural and sequential context of p53: A review of experimental and theoretical evidence.Prog Biophys Mol Biol. 2015 Mar;117(2-3):250-263. doi: 10.1016/j.pbiomolbio.2014.12.002. Epub 2014 Dec 27. Prog Biophys Mol Biol. 2015. PMID: 25550083 Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials
Miscellaneous