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

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 coll...

Täydet tiedot

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Bibliografiset tiedot
Päätekijät: Pollack, Lois, Tate, Mark W., Darnton, Nicholas C., Knight, James B., Gruner, Sol M., Eaton, William A., Austin, Robert H.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: The National Academy of Sciences 1999
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Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC17851/
https://ncbi.nlm.nih.gov/pubmed/10468571
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