ArticleEuropean biophysics journal : EBJ2023
Rethinking the protein folding problem from a new perspective.
Article in European biophysics journal : EBJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Fold-Switching Proteins.Annual review of biophysics · 2026Review
- Probing the Small, Medium and Large Amplitude Rheological Properties of Cherry Jell-OGels (Basel, Switzerland) · 2026Article
- Factors controlling protein evolvability-at the molecular scale.European biophysics journal : EBJ · 2026Article
- Fold-switching proteins.ArXiv · 2025Article
- The phase-seeding method for solving non-centrosymmetric crystal structures: a challenge for artificial intelligence.Acta crystallographica. Section A, Foundations and advances · 2025Article
- The origin of mutational epistasis.European biophysics journal : EBJ · 2024Article
- Analysis of proteins in the light of mutations.European biophysics journal : EBJ · 2024Review
- From cancer therapy to cardiac safety: the role of proteostasis in drug-induced cardiotoxicity.Frontiers in pharmacology · 2024Review
- Einstein Model of a Graph to Characterize Protein Folded/Unfolded States.Molecules (Basel, Switzerland) · 2023Article
- Protein structure prediction from the complementary science perspective.Biophysical reviews · 2023Article
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Authors and funding
1 author.
Funding
Abstract
One of the main concerns of Anfinsen was to reveal the connection between the amino-acid sequence and their biologically active conformation. This search gave rise to two crucial questions in structural biology, namely, why the proteins fold and how a sequence encodes its folding. As to the why, he proposes a plausible answer, namely, the thermodynamic hypothesis. As to the how, this remains an unsolved challenge. Consequently, the protein folding problem is examined here from a new perspective, namely, as an 'analytic whole'. Conceiving the protein folding in this way enabled us to (i) examine in detail why the force-field-based approaches have failed, among other purposes, in their ability to predict the three-dimensional structure of a protein accurately; (ii) propose how to redefine them to prevent these shortcomings, and (iii) conjecture on the origin of the state-of-the-art numerical-methods success to predict the tridimensional structure of proteins accurately.
Indexed as
Identifiers
37165178What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.