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Folding Kinetics of Staphylococcal Nuclease Studied by Tryptophan Engineering and Rapid Mixing Methods

To monitor the development of tertiary structural contacts during folding, a unique tryptophan residue was introduced at seven partially buried locations (residues 15, 27, 61, 76, 91, 102 and 121) of a tryptophan-free variant of staphylococcal nuclease (P47G/P117G/H124L/W140H). Thermal unfolding mea...

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Autors principals: Maki, Kosuke, Cheng, Hong, Dolgikh, Dimitry A., Roder, Heinrich
Format: Artigo
Idioma:Inglês
Publicat: 2007
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1892619/
https://ncbi.nlm.nih.gov/pubmed/17331534
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2007.02.006
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