Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy.
Proc Natl Acad Sci U S A
; 104(19): 7916-21, 2007 May 08.
Article
en En
| MEDLINE
| ID: mdl-17470816
ABSTRACT
We unfold and extend single proteins at a high force and then linearly relax the force to probe their collapse mechanisms. We observe a large variability in the extent of their recoil. Although chain entropy makes a small contribution, we show that the observed variability results from hydrophobic interactions with randomly varying magnitude from protein to protein. This collapse mechanism is common to highly extended proteins, including nonfolding elastomeric proteins like PEVK from titin. Our observations explain the puzzling differences between the folding behavior of highly extended proteins, from those folding after chemical or thermal denaturation. Probing the collapse of highly extended proteins with force spectroscopy allows separation of the different driving forces in protein folding.
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Bases de datos:
MEDLINE
Asunto principal:
Pliegue de Proteína
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2007
Tipo del documento:
Article
País de afiliación:
Estados Unidos