Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer.
Biophys J
; 93(1): 218-24, 2007 Jul 01.
Article
en En
| MEDLINE
| ID: mdl-17416618
ABSTRACT
We demonstrate that the sub-millisecond protein folding process referred to as "collapse" actually consists of at least two separate processes. We observe the UV fluorescence spectrum from naturally occurring tryptophans in three well-studied proteins, cytochrome c, apomyoglobin, and lysozyme, as a function of time in a microfluidic mixer with a dead time of approximately 20 mus. Single value decomposition of the time-dependent spectra reveal two separate processes 1), a spectral shift which occurs within the mixing time; and 2), a fluorescence decay occurring between approximately 100 and 300 micros. We attribute the first process to hydrophobic collapse and the second process to the formation of the first native tertiary contacts.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Modelos Moleculares
/
Pliegue de Proteína
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Microfluídica
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Modelos Químicos
Idioma:
En
Revista:
Biophys J
Año:
2007
Tipo del documento:
Article
País de afiliación:
Estados Unidos