ArticleThe Journal of biological chemistry2011
The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Dissecting the Structural Features of Folding Asymmetry and Transient Misfolding in a Multidomain PDZ Scaffold.Small science · 2026Article
- Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins.Biology direct · 2025Article
- Aromatic-aromatic interactions drive fold switch of GA95 and GB95 with three residue difference.Chemical science · 2025Article
- New GO-based measures in multiple network alignment.Bioinformatics (Oxford, England) · 2024Article
- SANA: cross-species prediction of Gene Ontology GO annotations via topological network alignment.NPJ systems biology and applications · 2022Article
- Article
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Shared unfolding pathways of unrelated immunoglobulin-like β-sandwich proteins.Protein engineering, design & selection : PEDS · 2019Article
- Investigating the Molecular Basis of the Aggregation Propensity of the Pathological D76N Mutant of Beta-2 Microglobulin: Role of the Denatured State.International journal of molecular sciences · 2019Article
- Insights from molecular dynamics simulations for computational protein design.Molecular systems design & engineering · 2017Article
- Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches.PLoS computational biology · 2016Article
- Insights into Unfolded Proteins from the Intrinsic ϕ/ψ Propensities of the AAXAA Host-Guest Series.Biophysical journal · 2016Article
- Studying protein fold evolution with hybrids of differently folded homologs.Protein engineering, design & selection : PEDS · 2015Article
- Proteinquakes in the evolution of influenza virus hemagglutinin (A/H1N1) under opposing migration and vaccination pressures.BioMed research international · 2015Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- HASH: a program to accurately predict protein Hα shifts from neighboring backbone shifts.Journal of biomolecular NMR · 2013Article
- Folding pathways of proteins with increasing degree of sequence identities but different structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Designing redox potential-controlled protein switches based on mutually exclusive proteins.Protein science : a publication of the Protein Society · 2012Article
- Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop end.Biochemistry · 2012Article
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7 authors.
Funding
Abstract
The protein folding problem is often studied by comparing the mechanisms of proteins sharing the same structure but different sequence. The recent design of the two proteins G(A)88 and G(B)88, displaying different structures and functions while sharing 88% sequence identity (49 out of 56 amino acids), allows the unique opportunity for a complementary approach. At which stage of its folding pathway does a protein commit to a given topology? Which residues are crucial in directing folding mechanisms to a given structure? By using a combination of biophysical and computational techniques, we have characterized the folding of both G(A)88 and G(B)88. We show that, contrary to expectation, G(B)88, characterized by a native α+β fold, displays in the denatured state a content of native-like helical structure greater than G(A)88, which is all-α in its native state. Both experiments and simulations indicate that such residual structure may be tuned by changing pH. Thus, despite the high sequence identity, the folding pathways for these two proteins appear to diverge as early as in the denatured state. Our results suggest a mechanism whereby protein topology is committed very early along the folding pathway, being imprinted in the residual structure of the denatured state.
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