A small fraction of all protein structures characterized so far are entangled. The challenge of understanding the properties of these knotted proteins, and the why and the how of their natural folding process, has been taken up in the past decade with different approaches, such as structural characterization, in vitro experiments, and simulations of protein models with varying levels of complexity. The simplest among these are the lattice Gō models, which belong to the class of structure-based models, i.e., models that are biased to the native structure by explicitly including structural data. In this review we highlight the contributions to the field made in the scope of lattice Gō models, putting them into perspective in the context of the main experimental and theoretical results and of other, more realistic, computational approaches.
{"title":"Knotted proteins: Tie etiquette in structural\u0000 biology","authors":"A. Nunes, P. F. Faísca","doi":"10.1090/conm/746/15007","DOIUrl":"https://doi.org/10.1090/conm/746/15007","url":null,"abstract":"A small fraction of all protein structures characterized so far are entangled. The challenge of understanding the properties of these knotted proteins, and the why and the how of their natural folding process, has been taken up in the past decade with different approaches, such as structural characterization, in vitro experiments, and simulations of protein models with varying levels of complexity. The simplest among these are the lattice Gō models, which belong to the class of structure-based models, i.e., models that are biased to the native structure by explicitly including structural data. In this review we highlight the contributions to the field made in the scope of lattice Gō models, putting them into perspective in the context of the main experimental and theoretical results and of other, more realistic, computational approaches.","PeriodicalId":297133,"journal":{"name":"Topology and Geometry of Biopolymers","volume":"171 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"117297873","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Focusing on a small set of proteins that i) fold in a concerted, all-or-none fashion and ii) do not contain knots or slipknots, we show that the Gauss linking integral, the torsion and the number of sequence-distant contacts provide information regarding the folding rate. Our results suggest that the global topology/geometry of the proteins shifts from right-handed to left-handed with decreasing folding rate, and that this topological change is associated with an increase in the number of more sequence-distant contacts.
{"title":"A topological study of protein folding\u0000 kinetics","authors":"E. Panagiotou, K. Plaxco","doi":"10.1090/conm/746/15010","DOIUrl":"https://doi.org/10.1090/conm/746/15010","url":null,"abstract":"Focusing on a small set of proteins that i) fold in a concerted, all-or-none fashion and ii) do not contain knots or slipknots, we show that the Gauss linking integral, the torsion and the number of sequence-distant contacts provide information regarding the folding rate. Our results suggest that the global topology/geometry of the proteins shifts from right-handed to left-handed with decreasing folding rate, and that this topological change is associated with an increase in the number of more sequence-distant contacts.","PeriodicalId":297133,"journal":{"name":"Topology and Geometry of Biopolymers","volume":"14 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128284591","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Site-specific recombination is an enzymatic process where two sites of precise sequence and orientation along a circle come together, are cleaved, and the ends are recombined. Site-specific recombination on a knotted substrate produces another knot or a two-component link depending on the relative orientation of the sites prior to recombination. Mathematically, site-specific recombination is modeled as coherent (knot to link) or non-coherent (knot to knot) banding. We here survey recent developments in the study of non-coherent bandings on knots and discuss biological implications.
{"title":"Recent advances on the non-coherent band\u0000 surgery model for site-specific\u0000 recombination","authors":"Allison H. Moore, M. Vázquez","doi":"10.1090/conm/746/15004","DOIUrl":"https://doi.org/10.1090/conm/746/15004","url":null,"abstract":"Site-specific recombination is an enzymatic process where two sites of precise sequence and orientation along a circle come together, are cleaved, and the ends are recombined. Site-specific recombination on a knotted substrate produces another knot or a two-component link depending on the relative orientation of the sites prior to recombination. Mathematically, site-specific recombination is modeled as coherent (knot to link) or non-coherent (knot to knot) banding. We here survey recent developments in the study of non-coherent bandings on knots and discuss biological implications.","PeriodicalId":297133,"journal":{"name":"Topology and Geometry of Biopolymers","volume":"3 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127745127","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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