Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding
AUTOR(ES)
Kitahara, Ryo
FONTE
The National Academy of Sciences
RESUMO
Atomic detailed structural study of a transiently existing folding intermediate is severely limited because of its short life. In ubiquitin, we found that a pressure-stabilized equilibrium conformer shares a common structural feature with the proline-trapped kinetic intermediate found in a pulse-labeling 1H/2H exchange NMR study [Briggs, M. S. & Roder, H. (1992) Proc. Natl. Acad. Sci. USA 89, 2017–2021]. The conformer is locally unfolded in the entire segment from residues 33 to 42 and in C-terminal residues 70–76. The close structural identity of an equilibrium intermediate stabilized under pressure with a transiently observed folding intermediate is likely to be general in terms of a folding funnel common to both experiments.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=152264Documentos Relacionados
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