ArticlePloS one2011
A coarse-grained approach to protein design: learning from design to understand folding.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Designing proteins: Mimicking natural protein sequence heterogeneity.The Journal of chemical physics · 2024Article
- From System Modeling to System Analysis: The Impact of Resolution Level and Resolution Distribution in the Computer-Aided Investigation of Biomolecules.Frontiers in molecular biosciences · 2021Review
- Engineering Proteins at Interfaces: From Complementary Characterization to Material Surfaces with Designed Functions.Angewandte Chemie (International ed. in English) · 2018Review
- Implementing efficient concerted rotations using Mathematica and C codeThe European physical journal. E, Soft matter · 2018Article
- The role of directional interactions in the designability of generalized heteropolymers.Scientific reports · 2017Article
- Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations.PLoS computational biology · 2015Article
- Article
- A simple lattice model that captures protein folding, aggregation and amyloid formation.PloS one · 2014Article
- Validating a Coarse-Grained Potential Energy Function through Protein Loop Modelling.PloS one · 2013Article
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Computational studies have given a great contribution in building our current understanding of the complex behavior of protein molecules; nevertheless, a complete characterization of their free energy landscape still represents a major challenge. Here, we introduce a new coarse-grained approach that allows for an extensive sampling of the conformational space of a large number of sequences. We explicitly discuss its application in protein design, and by studying four representative proteins, we show that the method generates sequences with a relatively smooth free energy surface directed towards the target structures.
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Registered trials
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