ArticleBiophysical journal2003
A minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native state.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- RedMDStream: Parameterization and Simulation Toolbox for Coarse-Grained Molecular Dynamics Models.Biophysical journal · 2015Article
- Combining coarse-grained protein models with replica-exchange all-atom molecular dynamics.International journal of molecular sciences · 2013Article
- Coarse-grained modeling of mucus barrier properties.Biophysical journal · 2012Article
- Coarse-grained Monte Carlo simulations of mucus: structure, dynamics, and thermodynamics.Biophysical journal · 2010Article
- An adaptive bin framework search method for a beta-sheet protein homopolymer model.BMC bioinformatics · 2007Article
- Inferring ideal amino acid interaction forms from statistical protein contact potentials.Proteins · 2005Article
- Ab initio protein structure prediction using pathway models.Comparative and functional genomics · 2003Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A simple protein model restricted to the face-centered cubic lattice has been studied. The model interaction scheme includes attractive interactions between hydrophobic (H) residues, repulsive interactions between hydrophobic and polar (P) residues, and orientation-dependent P-P interactions. Additionally, there is a potential that favors extended beta-type conformations. A sequence has been designed that adopts a native structure, consisting of an antiparallel, six-member Greek-key beta-barrel with protein-like structural degeneracy. It has been shown that the proposed model is a minimal one, i.e., all the above listed types of interactions are necessary for cooperative (all-or-none) type folding to the native state. Simulations were performed via the Replica Exchange Monte Carlo method and the numerical data analyzed via a multihistogram method.
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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.