Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants

Under mildly acidic conditions (pH 4–4.5) apomyoglobin (apoMb) adopts a partially structured equilibrium state (M-state) that structurally resembles a kinetic intermediate encountered at a late stage of folding to the native structure at neutral pH. We have previously reported that the M-state is fo...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2018-12, Vol.122 (49), p.11228-11239
Main Authors: Mizukami, Takuya, Xu, Ming, Fazlieva, Ruzaliya, Bychkova, Valentina E, Roder, Heinrich
Format: Article
Language:English
Subjects:
Animals
Apoproteins - chemistry
Apoproteins - genetics
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Kinetics
Mutagenesis, Site-Directed
Mutation
Myoglobin - chemistry
Myoglobin - genetics
Protein Conformation, alpha-Helical
Protein Unfolding
Sperm Whale
Thermodynamics
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Summary:Under mildly acidic conditions (pH 4–4.5) apomyoglobin (apoMb) adopts a partially structured equilibrium state (M-state) that structurally resembles a kinetic intermediate encountered at a late stage of folding to the native structure at neutral pH. We have previously reported that the M-state is formed rapidly (
ISSN:1520-6106
1520-5207
DOI:10.1021/acs.jpcb.8b06895