ArticleProtein science : a publication of the Protein Society2009
How strong are side chain interactions in the folding intermediate?
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 24 citations in OpenAlex.
- Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.Molecules (Basel, Switzerland) · 2023Article
- Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase ofBiomolecules · 2023Article
- The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.Molecules (Basel, Switzerland) · 2022Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.Biophysical journal · 2017Article
- Article
- The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Biophysical reviews · 2013Review
- 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
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influence of 12 nonpolar amino acids residues from the hydrophobic core of apomyoglobin on stability of its native state and folding intermediate was studied. Six of the selected residues are from the A, G and H helices; these are conserved in structure of the globin family, although nonfunctional, that is, not involved in heme binding. The rest are nonconserved hydrophobic residues that belong to the B, C, D, and E helices. Each residue was substituted by alanine, and equilibrium pH-induced transitions in apomyoglobin and its mutants were studied by circular dichroism and fluorescent spectroscopy. The obtained results allowed estimating changes in their free energy during formation of the intermediate state. It was first shown that the strength of side chain interactions in the apomyoglobin intermediate state amounts to 15-50% of that in its native state for conserved residues, and practically to 0% for nonconserved residues. These results allow a better understanding of interactions occurring in the intermediate state and shed light on involvement of certain residues in protein folding at different stages.
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