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Structural characterization of partially folded intermediates of apomyoglobin H64F

We present a detailed investigation of unfolded and partially folded states of a mutant apomyoglobin (apoMb) where the distal histidine has been replaced by phenylalanine (H64F). Previous studies have shown that substitution of His64, located in the E helix of the native protein, stabilizes the equi...

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שמור ב:
מידע ביבליוגרפי
Main Authors: Schwarzinger, Stephan, Mohana-Borges, Ronaldo, Kroon, Gerard J.A., Dyson, H. Jane, Wright, Peter E.
פורמט: Artigo
שפה:Inglês
יצא לאור: Cold Spring Harbor Laboratory Press 2008
נושאים:
גישה מקוונת:https://ncbi.nlm.nih.gov/pmc/articles/PMC2222724/
https://ncbi.nlm.nih.gov/pubmed/18227434
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.073187208
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