PuSH - Publikationsserver des Helmholtz Zentrums München: CONRAD: A method for identification of variable and conserved regions within proteins by scale-space filtering.

Informationen

Hinweise zu Qualitätskriterien von Zeitschriften

Open-Access-Richtlinie der Helmholtz-Gemeinschaft 2016

CC Licencences

Metriken für Publikationen

Navigation

Startseite

English

EVA: Veröffentlichen

Neuer EVA Antrag

Recherche

Erweiterte Suche

Durchblättern nach ...

... HMGU-Autoren/Konsortien

... Organisationsstruktur

... Zeitschriften

... Publikationstypen

... Forschungsdaten

... Arbeitsgruppen

... Erscheinungsjahr

Publikationen im Überblick

Statistik

HGF Fortschrittsbericht

OA Publikationen

Eintragen

Neue Publikation eintragen

Neue Publikation holen aus...

...EVA

Fehlende Publikation melden

Highlights

Suche

Hilfe & Kontakt

Ansprechpartner

Hilfe

Datenschutz

Helmholtz Open Science

Bibliometrische Indikatoren

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Herrmann, G. ; Schön, A. ; Brack-Werner, R. ; Werner, T.

CONRAD: A method for identification of variable and conserved regions within proteins by scale-space filtering.

Bioinformatics 12, 197-203 (1996)

Verlagsversion

DOI

	Open Access Gold

Abstract
Metriken
Zusatzinfos

Advanced sequencing techniques allow rapid deduction of individual amino acid sequences of highly related proteins. Due to their quasi-species nature, viral genomes (e.g. HIV-1) represent one of the most common sources of related proteins. Another example of related proteins are immunoglobulins. Local differences in amino acid conservation are useful indicators of potential domain structures and immunological or functional epitopes prior to structural analysis of proteins. Although variability indices can be calculated by several methods, delineation of boundaries between sequence stretches with similar variability indices is left to the user. We use algorithmic scale-space filtering for delineation of conserved and variable sequence stretches within a protein which is performed on an algorithmic basis avoiding arbitrary assignments. Our method correctly identified variable regions for the human immunoglobulin λ-chain V-regions (subgroup I). Prediction of the variable regions of the HIV-1 gp120 env protein was in agreement with empirical derived definitions. These examples indicate that our method is useful for the regional assignment of protein variability solely on the basis of amino acid sequences.

Impact Factor

Scopus SNIP

Scopus
Cited By

Altmetric

0.000