About: Hopp–Woods scale     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : yago:WikicatProteins, within Data Space : dbpedia.demo.openlinksw.com associated with source document(s)
QRcode icon
http://dbpedia.demo.openlinksw.com/describe/?url=http%3A%2F%2Fdbpedia.org%2Fresource%2FHopp%E2%80%93Woods_scale&invfp=IFP_OFF&sas=SAME_AS_OFF

The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA. Given the amino acid sequence of any protein, likely interaction sites can be identified by taking the moving average of six amino acid hydrophilicity values along the polypeptide chain, and looking for local peaks in the data plot. * v * t * e

AttributesValues
rdf:type
rdfs:label
  • Hopp–Woods scale (en)
rdfs:comment
  • The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA. Given the amino acid sequence of any protein, likely interaction sites can be identified by taking the moving average of six amino acid hydrophilicity values along the polypeptide chain, and looking for local peaks in the data plot. * v * t * e (en)
dcterms:subject
Wikipage page ID
Wikipage revision ID
Link from a Wikipage to another Wikipage
sameAs
dbp:wikiPageUsesTemplate
has abstract
  • The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA. Given the amino acid sequence of any protein, likely interaction sites can be identified by taking the moving average of six amino acid hydrophilicity values along the polypeptide chain, and looking for local peaks in the data plot. In subsequent papers after their initial publication of the method, Hopp and Woods demonstrated that the data plots, or hydrophilicity profiles, contained much information about protein folding, and that the of the profiles corresponded to internal structures of proteins such as beta-strands and alpha-helices. Furthermore, long hydrophobic valleys were shown to correspond quite closely to the membrane-spanning helices identified by the later-published Kyte and Doolittle method. * v * t * e (en)
gold:hypernym
prov:wasDerivedFrom
page length (characters) of wiki page
foaf:isPrimaryTopicOf
is Link from a Wikipage to another Wikipage of
is Wikipage redirect of
is foaf:primaryTopic of
Faceted Search & Find service v1.17_git139 as of Feb 29 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 08.03.3330 as of Mar 19 2024, on Linux (x86_64-generic-linux-glibc212), Single-Server Edition (378 GB total memory, 59 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software