Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy.
Protein Sci
; 21(11): 1682-8, 2012 Nov.
Article
in En
| MEDLINE
| ID: mdl-22915551
It has been estimated that 30% of eukaryotic protein and 70% of transcription factors are intrinsically disordered (ID). The biochemical significance of proteins that lack stable tertiary structure, however, is not clearly understood, largely owing to an inability to assign well-defined structures to specific biological tasks. In an attempt to investigate the structural character of ID protein, we have measured the circular dichroism spectrum of the N-terminal region of p53 over a range of temperatures and solution conditions. p53 is a well-studied transcription factor that has a proline-rich N-terminal ID region containing two activation domains. High proline content is a property commonly associated with ID, and thus p53 may be a good model system for investigating the biochemical importance of ID. The spectra presented here suggest that the N-terminal region of p53 may adopt an ordered structure under physiological conditions and that this structure can be thermally unfolded in an apparent two-state manner. The midpoint temperature for this thermal unfolding of the N-terminal region of p53 was at the near-physiological temperature of 39°C, suggesting the possibility of a physiological role for the observed structural equilibrium.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Tumor Suppressor Protein p53
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Protein Sci
Journal subject:
BIOQUIMICA
Year:
2012
Document type:
Article
Affiliation country:
United States
Country of publication:
United States