Artigo Revisado por pares

Thermal stability of proteins

1973; Elsevier BV; Volume: 158; Issue: 2 Linguagem: Inglês

10.1016/0003-9861(73)90561-4

ISSN

1096-0384

Autores

Henry B. Bull, Keith Breese,

Tópico(s)

Protein purification and stability

Resumo

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.

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