ArticleJournal of molecular biology2011
Characterizing the existing and potential structural space of proteins by large-scale multiple loop permutations.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- SplitSeek-Pro: accurate prediction of splittable sites on protein structures.Nature communications · 2026Article
- Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Deep generative models of protein structure uncover distant relationships across a continuous fold space.Nature communications · 2024Article
- A review of visualisations of protein fold networks and their relationship with sequence and function.Biological reviews of the Cambridge Philosophical Society · 2023Review
- Sixty-five years of the long march in protein secondary structure prediction: the final stretch?Briefings in bioinformatics · 2018Article
- Rules for connectivity of secondary structure elements in protein: Two-layer αβ sandwiches.Protein science : a publication of the Protein Society · 2017Article
- Article
- Protein rethreading: A novel approach to protein design.Scientific reports · 2016Article
- Biophysics of protein evolution and evolutionary protein biophysics.Journal of the Royal Society, Interface · 2014Article
- Article
- LEAP: highly accurate prediction of protein loop conformations by integrating coarse-grained sampling and optimized energy scores with all-atom refinement of backbone and side chains.Journal of computational chemistry · 2014Article
- How a spatial arrangement of secondary structure elements is dispersed in the universe of protein folds.PloS one · 2014Article
- Energy functions in de novo protein design: current challenges and future prospects.Annual review of biophysics · 2013Review
- Article
- Further evidence for the likely completeness of the library of solved single domain protein structures.The journal of physical chemistry. B · 2012Article
- Template-based structure prediction and classification of transcription factors in Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2012Article
- Why not consider a spherical protein? Implications of backbone hydrogen bonding for protein structure and function.Physical chemistry chemical physics : PCCP · 2011Article
- Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of query and corresponding native properties of templates.Bioinformatics (Oxford, England) · 2011Article
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Authors and funding
2 authors.
Funding
Abstract
Worldwide structural genomics projects are increasing structure coverage of sequence space but have not significantly expanded the protein structure space itself (i.e., number of unique structural folds) since 2007. Discovering new structural folds experimentally by directed evolution and random recombination of secondary-structure blocks is also proved rarely successful. Meanwhile, previous computational efforts for large-scale mapping of protein structure space are limited to simple model proteins and led to an inconclusive answer on the completeness of the existing observed protein structure space. Here, we build novel protein structures by extending naturally occurring circular (single-loop) permutation to multiple loop permutations (MLPs). These structures are clustered by structural similarity measure called TM-score. The computational technique allows us to produce different structural clusters on the same naturally occurring, packed, stable core but with alternatively connected secondary-structure segments. A large-scale MLP of 2936 domains from structural classification of protein domains reproduces those existing structural clusters (63%) mostly as hubs for many nonredundant sequences and illustrates newly discovered novel clusters as islands adopted by a few sequences only. Results further show that there exist a significant number of novel potentially stable clusters for medium-size or large-size single-domain proteins, in particular, >100 amino acid residues, that are either not yet adopted by nature or adopted only by a few sequences. This study suggests that MLP provides a simple yet highly effective tool for engineering and design of novel protein structures (including naturally knotted proteins). The implication of recovering new-fold targets from critical assessment of structure prediction techniques (CASP) by MLP on template-based structure prediction is also discussed. Our MLP structures are available for download at the publication page of the Web site http://sparks.informatics.iupui.edu.
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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.