ArticleInternational journal of molecular sciences2011
Intermediates in the protein folding process: a computational model.
Article in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.International journal of molecular sciences · 2018Article
- Statistical dictionaries for hypothetical in silico model of the early-stage intermediate in protein folding.Journal of computer-aided molecular design · 2015Article
- Contingency Table Browser - prediction of early stage protein structure.Bioinformation · 2015Article
- Hypothetical in silico model of the early-stage intermediate in protein folding.Journal of molecular modeling · 2013Article
- The effect of C-terminal helix on the stability of FF domain studied by molecular dynamics simulation.International journal of molecular sciences · 2012Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The paper presents a model for simulating the protein folding process in silico. The two-step model (which consists of the early stage-ES and the late stage-LS) is verified using two proteins, one of which is treated (according to experimental observations) as the early stage and the second as an example of the LS step. The early stage is based solely on backbone structural preferences, while the LS model takes into account the water environment, treated as an external hydrophobic force field and represented by a 3D Gauss function. The characteristics of 1ZTR (the ES intermediate, as compared with 1ENH, which is the LS intermediate) confirm the link between the gradual disappearance of ES characteristics in LS structural forms and the simultaneous emergence of LS properties in the 1ENH protein. Positive verification of ES and LS characteristics in these two proteins (1ZTR and 1ENH respectively) suggest potential applicability of the presented model to in silico protein folding simulations.
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