Ropelength of tight polygonal knots

A physical interpretation of the rope simulated by the SONO algorithm is presented. Properties of the tight polygonal knots delivered by the algorithm are analyzed. An algorithm for bounding the ropelength of a smooth inscribed knot is shown. Two ways of calculating the ropelength of tight polygonal knots are compared. An analytical calculation performed for a model knot shows that an appropriately weighted average should provide a good estimation of the minimum ropelength for relatively small numbers of edges.Comment: 27 pages, to appear in "Physical and Numerical Models in Knot Theory and their Application to the Life Sciences

Knot Fertility and Lineage

In this paper, we introduce a new type of relation between knots called the descendant relation. One knot $H$ is a descendant of another knot $K$ if $H$ can be obtained from a minimal crossing diagram of $K$ by some number of crossing changes. We explore properties of the descendant relation and study how certain knots are related, paying particular attention to those knots, called fertile knots, that have a large number of descendants. Furthermore, we provide computational data related to various notions of knot fertility and propose several open questions for future exploration.Comment: 20 pages, 11 figures, 14 table

Shapes of Knotted Cyclic Polymers(Knots and soft-matter physics: Topology of polymers and related topics in physics, mathematics and biology)

この論文は国立情報学研究所の電子図書館事業により電子化されました。Momentary configurations of long polymers at thermal equilibrium usually deviate from spherical symmetry and can be better described, on average, by a prolate ellipsoid. The asphericity and nature of asphericity (or prolateness) that describe these momentary ellipsoidal shapes of a polymer are determined by specific expressions involving the three principal moments of inertia calculated for configurations of the polymer. Earlier theoretical studies and numerical simulations have established that as the length of the polymer increases, the average shape for the statistical ensemble of random configurations asymptotically approaches a characteristic universal shape that depends on the solvent quality. It has been established, however, that these universal shapes differ for linear, circular, and branched chains. We investigate here the effect of knotting on the shape of cyclic polymers modeled as random isosegmental polygons. We observe that random polygons forming different knot types reach asymptotic shapes that are distinct from the ensemble average shape. For the same chain length, more complex knots are, on average, more spherical than less complex knots. This paper is a shorter, revised version of the article Ref. [12]. For more details, see Ref. [12]

Bending modes of DNA directly addressed by cryo-electron microscopy of DNA minicircles

We use cryo-electron microscopy (cryo-EM) to study the 3D shapes of 94-bp-long DNA minicircles and address the question of whether cyclization of such short DNA molecules necessitates the formation of sharp, localized kinks in DNA or whether the necessary bending can be redistributed and accomplished within the limits of the elastic, standard model of DNA flexibility. By comparing the shapes of covalently closed, nicked and gapped DNA minicircles, we conclude that 94-bp-long covalently closed and nicked DNA minicircles do not show sharp kinks while gapped DNA molecules, containing very flexible single-stranded regions, do show sharp kinks. We corroborate the results of cryo-EM studies by using Bal31 nuclease to probe for the existence of kinks in 94-bp-long minicircle

KnotProt: a database of proteins with knots and slipknots

The protein topology database KnotProt, http://knotprot.cent.uw.edu.pl/, collects information about protein structures with open polypeptide chains forming knots or slipknots. The knotting complexity of the cataloged proteins is presented in the form of a matrix diagram that shows users the knot type of the entire polypeptide chain and of each of its subchains. The pattern visible in the matrix gives the knotting fingerprint of a given protein and permits users to determine, for example, the minimal length of the knotted regions (knot's core size) or the depth of a knot, i.e. how many amino acids can be removed from either end of the cataloged protein structure before converting it from a knot to a different type of knot. In addition, the database presents extensive information about the biological functions, families and fold types of proteins with non-trivial knotting. As an additional feature, the KnotProt database enables users to submit protein or polymer chains and generate their knotting fingerprint

LinkProt : a database collecting information about biological links

Protein chains are known to fold into topologically complex shapes, such as knots, slipknots or complex lassos. This complex topology of the chain can be considered as an additional feature of a protein, separate from secondary and tertiary structures. Moreover, the complex topology can be defined also as one additional structural level. The LinkProt database (http://linkprot.cent.uw.edu.pl) collects and displays information about protein links - topologically non-trivial structures made by up to four chains and complexes of chains (e.g. in capsids). The database presents deterministic links (with loops closed, e.g. by two disulfide bonds), links formed probabilistically and macromolecular links. The structures are classified according to their topology and presented using the minimal surface area method. The database is also equipped with basic tools which allow users to analyze the topology of arbitrary (bio)polymers