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Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin

Excited states of proteins may play important roles in function, yet are difficult to study spectroscopically because of their sparse population. High hydrostatic pressure increases the equilibrium population of excited states, enabling their characterization [Akasaka K (2003) Biochemistry 42:10875–...

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Autores principales: Lerch, Michael T., Horwitz, Joseph, McCoy, John, Hubbell, Wayne L.
Formato: Artigo
Lenguaje:Inglês
Publicado: National Academy of Sciences 2013
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC3856799/
https://ncbi.nlm.nih.gov/pubmed/24248390
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1320124110
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