ArticleProceedings of the National Academy of Sciences of the United States of America2005
Protein-folding landscapes in multichain systems.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. 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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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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Who cites it
9 citing papers in PubMed, 46 citations in OpenAlex.
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- Free energy landscapes for initiation and branching of protein aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A coarse-grained protein model in a water-like solvent.Scientific reports · 2013Article
- Probing surface tension additivity on chemically heterogeneous surfaces by a molecular approach.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Thermal and structural stability of adsorbed proteins.Biophysical journal · 2010Article
- In silico protein fragmentation reveals the importance of critical nuclei on domain reassembly.Biophysical journal · 2008Article
- Protein aggregation in silico.Trends in biotechnology · 2007Review
- On the evolution of the standard amino-acid alphabet.Genome biology · 2006Article
- Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Computational studies of proteins have significantly improved our understanding of protein folding. These studies are normally carried out by using chains in isolation. However, in many systems of practical interest, proteins fold in the presence of other molecules. To obtain insight into folding in such situations, we compare the thermodynamics of folding for a Miyazawa-Jernigan model 64-mer in isolation to results obtained in the presence of additional chains. The melting temperature falls as the chain concentration increases. In multichain systems, free-energy landscapes for folding show an increased preference for misfolded states. Misfolding is accompanied by an increase in interprotein interactions; however, near the folding temperature, the transition from folded chains to misfolded and associated chains is entropically driven. A majority of the most probable interprotein contacts are also native contacts, suggesting that native topology plays a role in early stages of aggregation.
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