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Relaxation of Structural Constraints during Amicyanin Unfolding

We study the thermal unfolding of amicyanin by quantifying the resiliency of the native state to structural perturbations. Three signatures characterizing stages of unfolding are identified. The first signature, lateral extension of the polypeptide chain, is calculated directly from the reported cry...

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Détails bibliographiques
Publié dans:J Inorg Biochem
Auteurs principaux: Kozak, John J., Gray, Harry B., Garza-López, Roberto A.
Format: Artigo
Langue:Inglês
Publié: 2017
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC7222854/
https://ncbi.nlm.nih.gov/pubmed/29222970
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jinorgbio.2017.11.016
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