Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

Lois Pollack; Mark W. Tate; Nicholas C. Darnton; James B. Knight; Sol M. Gruner; William A. Eaton; Robert H. Austin

doi:10.1073/pnas.96.18.10115

Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

Lois Pollack, Mark W. Tate, Nicholas C. Darnton, James B. Knight, Sol M. Gruner, William A. Eaton, Robert H. Austin

Research output: Contribution to journal › Article › peer-review

277 Scopus citations

Abstract

Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.

Original language	English (US)
Pages (from-to)	10115-10117
Number of pages	3
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	96
Issue number	18
DOIs	https://doi.org/10.1073/pnas.96.18.10115
State	Published - Aug 31 1999

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Pollack, L., Tate, M. W., Darnton, N. C., Knight, J. B., Gruner, S. M., Eaton, W. A., & Austin, R. H. (1999). Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proceedings of the National Academy of Sciences of the United States of America, 96(18), 10115-10117. https://doi.org/10.1073/pnas.96.18.10115

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abstract = "Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.",

author = "Lois Pollack and Tate, \{Mark W.\} and Darnton, \{Nicholas C.\} and Knight, \{James B.\} and Gruner, \{Sol M.\} and Eaton, \{William A.\} and Austin, \{Robert H.\}",

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doi = "10.1073/pnas.96.18.10115",

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Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. / Pollack, Lois; Tate, Mark W.; Darnton, Nicholas C. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 18, 31.08.1999, p. 10115-10117.

Research output: Contribution to journal › Article › peer-review

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T1 - Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

AU - Pollack, Lois

AU - Tate, Mark W.

AU - Darnton, Nicholas C.

AU - Knight, James B.

AU - Gruner, Sol M.

AU - Eaton, William A.

AU - Austin, Robert H.

PY - 1999/8/31

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AB - Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.

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Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

Abstract

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