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A scanning calorimetric study of unfolding equilibria in homodimeric chicken gizzard tropomyosins.

Using both circular dichroism (CD) and differential scanning calorimetry (DSC), several laboratories find that the thermal unfolding transitions of alpha alpha and beta beta homodimeric coiled coils of rabbit tropomyosin are multistate and display an overall unfolding enthalpy of near 300 kcal (mol...

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Autores principales: O'Brien, R, Sturtevant, J M, Wrabl, J, Holtzer, M E, Holtzer, A
Formato: Artigo
Lenguaje:Inglês
Publicado: 1996
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1225217/
https://ncbi.nlm.nih.gov/pubmed/9172766
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