Literature DB >> 21086029

Planck-Benzinger thermal work function: thermodynamic characterization of the carboxy-terminus of p53 peptide fragments.

Paul W Chun1, Marc S Lewis.   

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.

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Year:  2010        PMID: 21086029     DOI: 10.1007/s10930-010-9286-9

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   2.371


  41 in total

1.  Deacetylation of p53 modulates its effect on cell growth and apoptosis.

Authors:  J Luo; F Su; D Chen; A Shiloh; W Gu
Journal:  Nature       Date:  2000-11-16       Impact factor: 49.962

2.  The oligomerization domain of p53: crystal structure of the trigonal form.

Authors:  M Miller; J Lubkowski; J K Rao; A T Danishefsky; J G Omichinski; K Sakaguchi; H Sakamoto; E Appella; A M Gronenborn; G M Clore
Journal:  FEBS Lett       Date:  1996-12-09       Impact factor: 4.124

3.  New thermodynamic studies on ribonuclease A at low pH.

Authors:  P W Chun
Journal:  J Biol Chem       Date:  1995-06-09       Impact factor: 5.157

4.  Solution structure of the tetrameric minimum transforming domain of p53.

Authors:  W Lee; T S Harvey; Y Yin; P Yau; D Litchfield; C H Arrowsmith
Journal:  Nat Struct Biol       Date:  1994-12

5.  p53 domains: structure, oligomerization, and transformation.

Authors:  P Wang; M Reed; Y Wang; G Mayr; J E Stenger; M E Anderson; J F Schwedes; P Tegtmeyer
Journal:  Mol Cell Biol       Date:  1994-08       Impact factor: 4.272

6.  Effect of phosphorylation on tetramerization of the tumor suppressor protein p53.

Authors:  K Sakaguchi; H Sakamoto; D Xie; J W Erickson; M S Lewis; C W Anderson; E Appella
Journal:  J Protein Chem       Date:  1997-07

Review 7.  Post-translational modification of p53 in tumorigenesis.

Authors:  Ann M Bode; Zigang Dong
Journal:  Nat Rev Cancer       Date:  2004-10       Impact factor: 60.716

Review 8.  The p53 family and programmed cell death.

Authors:  E C Pietsch; S M Sykes; S B McMahon; M E Murphy
Journal:  Oncogene       Date:  2008-10-27       Impact factor: 9.867

Review 9.  The P53 pathway: what questions remain to be explored?

Authors:  A J Levine; W Hu; Z Feng
Journal:  Cell Death Differ       Date:  2006-06       Impact factor: 15.828

10.  Refined solution structure of the oligomerization domain of the tumour suppressor p53.

Authors:  G M Clore; J Ernst; R Clubb; J G Omichinski; W M Kennedy; K Sakaguchi; E Appella; A M Gronenborn
Journal:  Nat Struct Biol       Date:  1995-04
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