ArticleProtein science : a publication of the Protein Society2005
Three-state protein folding: experimental determination of free-energy profile.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.Molecules (Basel, Switzerland) · 2023Article
- Characterization of Cyclophilin from ThaumarchaeotaACS omega · 2022Article
- Some useful ideas for multistate protein design: Effect of amino acid substitutions on the multistate proteins stability and the rate of protein structure formation.Frontiers in molecular biosciences · 2022Article
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.Biophysical journal · 2019Article
- sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.Biophysical journal · 2017Article
- Human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine.The Journal of biological chemistry · 2014Article
- Article
- Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.Biophysical journal · 2010Article
- How strong are side chain interactions in the folding intermediate?Protein science : a publication of the Protein Society · 2009Article
- Cloning, purification and bioactivity assay of human CD28 single-chain antibody in Escherichia coli.Cytotechnology · 2009Article
- Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli.Photosynthesis researchArticle
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
When considering protein folding with a transient intermediate, a difficulty arises as to determination of the rates of separate transitions. Here we overcome this problem, using the kinetic studies of the unfolding/refolding reactions of the three-state protein apomyoglobin as a model. Amplitudes of the protein refolding kinetic burst phase corresponding to the transition from the unfolded (U) to intermediate (I) state, that occurs prior to the native state (N) formation, allow us to estimate relative populations of the rapidly converting states at various final urea concentrations. On the basis of these proportions, a complicated experimental chevron plot has been deconvolved into the urea-dependent rates of the I<-->N and U<-->N transitions to give the dependence of free energies of the main transition state and of all three (N, I, and U) stable states on urea concentration.
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