Zobrazeno 1 - 10
of 92
pro vyhledávání: '"Kenneth C Millett"'
The physical properties of knotted and linked configurations in space have long been of interest to mathematicians. More recently, these properties have become significant to biologists, physicists, and engineers among others. Their depth of importan
Autor:
Kenneth C. Millett, Eleni Panagiotou
Publikováno v:
Journal of Knot Theory and Its Ramifications.
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Geometry and topology are the main factors that determine the functional properties of proteins. In this work, we show how to use the Gauss linking integral (GLN) in the form of a matrix diagram - for a pair of a loop and a tail - to study both the g
Autor:
Piotr Sułkowski, Eric J. Rawdon, Pawel Rubach, Kenneth C. Millett, Joanna I. Sulkowska, Andrzej Stasiak, Julien Dorier, Dimos Goundaroulis, Pawel Dabrowski-Tumanski
Publikováno v:
Nucleic Acids Research
Nucleic acids research, vol. 47, no. D1, pp. D367-D375
Nucleic acids research, vol 47, iss D1
Nucleic acids research, vol. 47, no. D1, pp. D367-D375
Nucleic acids research, vol 47, iss D1
The KnotProt 2.0 database (the updated version of the KnotProt database) collects information about proteins which form knots and other entangled structures. New features in KnotProt 2.0 include the characterization of both probabilistic and determin
Autor:
Kenneth C. Millett
Publikováno v:
Reactive and Functional Polymers. 131:181-190
In the 1980’s, knotting in DNA became a fundamental research dimension in the study of the mechanisms by which enzymes act on it. Later, the first compelling identification of knotting in proteins, in 2000, launched the study of knotting in protein
Autor:
Pawel Dabrowski-Tumanski, Wanda Niemyska, Aleksandra Maria Gierut, Joanna I. Sulkowska, Kenneth C. Millett
Publikováno v:
Bioinformatics. 35:3166-3168
Summary Links are generalization of knots, that consist of several components. They appear in proteins, peptides and other biopolymers with disulfide bonds or ions interactions giving rise to the exceptional stability. Moreover because of this stabil
Autor:
Colin C. Adams, Cameron McA. Gordon, Vaughan F.R. Jones, Louis H. Kauffman, Sofia Lambropoulou, Kenneth C. Millett, Jozef H. Przytycki, Renzo Ricca, Radmila Sazdanovic
This proceedings volume presents a diverse collection of high-quality, state-of-the-art research and survey articles written by top experts in low-dimensional topology and its applications. The focal topics include the wide range of historical and c
Publikováno v:
Nucleic acids research
Nucleic acids research, vol 44, iss 10
Nucleic Acids Research
Nucleic acids research, vol. 44, no. 10, pp. 4528-4538
Nucleic acids research, vol 44, iss 10
Nucleic Acids Research
Nucleic acids research, vol. 44, no. 10, pp. 4528-4538
Freshly replicated DNA molecules initially form multiply interlinked right-handed catenanes. In bacteria, these catenated molecules become supercoiled by DNA gyrase before they undergo a complete decatenation by topoisomerase IV (Topo IV). Topo IV is
Publikováno v:
New Directions in Geometric and Applied Knot Theory ISBN: 9783110571493
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3492fe598f87b7c923e2af9c93b3fc39
https://doi.org/10.1515/9783110571493-011
https://doi.org/10.1515/9783110571493-011
Autor:
Aleksandra I. Jarmolinska, Kenneth C. Millett, Wanda Niemyska, Eric J. Rawdon, Joanna I. Sulkowska, Pawel Dabrowski-Tumanski
Publikováno v:
Dabrowski-Tumanski, P; Jarmolinska, AI; Niemyska, W; Rawdon, EJ; Millett, KC; & Sulkowska, JI. (2017). LinkProt: a database collecting information about biological links. NUCLEIC ACIDS RESEARCH, 45(D1), D243-D249. doi: 10.1093/nar/gkw976. UC Santa Barbara: Retrieved from: http://www.escholarship.org/uc/item/25q2r8p1
Nucleic acids research, vol 45, iss D1
Nucleic Acids Research
Nucleic acids research, vol 45, iss D1
Nucleic Acids Research
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 structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f0cda06236a861f9567adb8a9e6102
http://www.escholarship.org/uc/item/25q2r8p1
http://www.escholarship.org/uc/item/25q2r8p1