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Tytuł pozycji:

KnotProt: a database of proteins with knots and slipknots.

Tytuł:
KnotProt: a database of proteins with knots and slipknots.
Autorzy:
Jamroz M; Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
Niemyska W; Institute of Mathematics, University of Silesia, Bankowa 14, 40-007 Katowice, Poland.
Rawdon EJ; Department of Mathematics, University of St. Thomas, Saint Paul, MN 55105, USA.
Stasiak A; Center for Integrative Genomics, University of Lausanne, 1015-Lausanne, Switzerland .
Millett KC; Department of Mathematics, University of California, Santa Barbara, CA 93106, USA.
Sułkowski P; Faculty of Physics, University of Warsaw, Pasteura 5, 02-093 Warsaw, Poland California Institute of Technology, Pasadena, CA 91125, USA .
Sulkowska JI; Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland Centre of New Technologies, University of Warsaw, Banacha 2c, 02-097, Warsaw, Poland .
Źródło:
Nucleic acids research [Nucleic Acids Res] 2015 Jan; Vol. 43 (Database issue), pp. D306-14. Date of Electronic Publication: 2014 Oct 31.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
MeSH Terms:
Databases, Protein*
Protein Conformation*
Peptides/chemistry
References:
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Substance Nomenclature:
0 (Peptides)
Entry Date(s):
Date Created: 20141102 Date Completed: 20150629 Latest Revision: 20181113
Update Code:
20240104
PubMed Central ID:
PMC4383900
DOI:
10.1093/nar/gku1059
PMID:
25361973
Czasopismo naukowe
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 fingerprints.
(© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.)

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