ArticleThe journal of physical chemistry. B2012
Effects of two solvent conditions on the free energy landscape of the BBL peripheral subunit binding domain.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- pH-Dependent cooperativity and existence of a dry molten globule in the folding of a miniprotein BBL.Physical chemistry chemical physics : PCCP · 2018Article
- The Role of Electrostatic Interactions in Folding of β-Proteins.Journal of the American Chemical Society · 2016Article
- Recent development and application of constant pH molecular dynamics.Molecular simulation · 2014Article
- Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.PloS one · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
BBL is a small independently folding domain with two main parallel helices. The experiment of C(α) secondary shifts has shown that changing the pH from ~7 to ~5 results in the reduced helicity at the C-terminus of helix 2. Combining constant pH molecular dynamics with replica exchange, we sampled the protein conformation space and protonation states extensively under a neutral pH condition and an acidic condition. Our results reveal that the solvent conditions influence the free energy landscape. Under the neutral pH condition, the denatured state and the native state are well separated. The condition of the acidic pH reshapes the free energy surface, leading to a broadly populated denatured-state basin and a low free energy barrier between the denatured state and the native state. The acidic pH shifts the equilibrium between the denatured state and the native state in favor of the denatured state. Caution must be used to interpret experimental data under the acidic condition because the contribution of the denatured state is significant. Our simulation results are supported by the fact that the calculated chemical shifts are in good agreement with the experiment data.
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