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Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation

The equilibrium unfolding of the Formin binding protein 28 (FBP) WW domain, a stable three-stranded β-sheet protein, can be described as reversible apparent two-state folding. Kinetics studied by laser temperature jump reveal a third state at temperatures below the midpoint of unfolding. The FBP fre...

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Bibliographic Details
Main Authors: Nguyen, Houbi, Jäger, Marcus, Moretto, Alessandro, Gruebele, Martin, Kelly, Jeffery W.
Format: Artigo
Language:Inglês
Published: The National Academy of Sciences 2003
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC153028/
https://ncbi.nlm.nih.gov/pubmed/12651955
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0538054100
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