Thermal stability of proteins

The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960. The correlation coefficient between the average residue...

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Veröffentlicht in:Archives of biochemistry and biophysics 1973-10, Vol.158 (2), p.681-686
Hauptverfasser: Bull, Henry B., Breese, Keith
Format: Artikel
Sprache:eng
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Zusammenfassung:The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960. The correlation coefficient between the average residue volume and the hydrophobic index was +0.697. The least square relation between the melting points of the proteins and hydrophobic index and the average residue volumes considered as independent variables yielded a positive coefficient for the average residue volume and a negative coefficient for the hydrophobic index.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(73)90561-4