Artículo de revista
An examination of the involvement of proline peptide isomerization in protein folding
Fecha
1978Registro en:
Journal of Molecular Biology, Volumen 126, Issue 1, 2018, Pages 117-121
00222836
10.1016/0022-2836(78)90284-X
Autor
Babul Cattán, Jorge
Nakagawa, Allen
Stellwagen, Earle
Institución
Resumen
The proline peptide isomerization model of protein folding predicts that the fraction of denatured polypeptide chains which rapidly fold should be quantitatively related to the numbers of cis and trans proline residues in the folded polypeptide conformation. However, we find that neither the comparative nor the absolute kinetic pattern for folding of the homologous proteins, tuna heart and horse heart ferricytochrome c which differ by one proline residue, is compatible with the quantitative predictions of the proline peptide isomerization model. © 1978.