PuSH - Publikationsserver des Helmholtz Zentrums München: The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic.

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

Jacso, T. ; Bardiaux, B.* ; Broecker, J.* ; Fiedler, S.* ; Baerwinkel, T. ; Mainz, A.* ; Fink, U.* ; Vargas, C.* ; Oschkinat, H.* ; Keller, S.* ; Reif, B.

The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic.

J. Am. Chem. Soc. 135, 18884-18891 (2013)

DOI

PMC

Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

Abstract
Metriken
Zusatzinfos

In vitro protein-folding studies using chemical denaturants such as urea are indispensible in elucidating the forces and mechanisms determining the stability, structure, and dynamics of water-soluble proteins. By contrast, a-helical membrane-associated proteins largely evade such approaches because they are resilient to extensive unfolding We have used of the alpha-helical membrane-associated protein Mistic as well as dissection of the effects of urea on the structure and dynamics optical and NMR spectroscopy to provide an atomistic-level its interactions with detergent and solvent molecules. In the presence of the zwitterionic detergent lauryl dimethylamine oxide, increasing concentrations of urea result in a complex sequence of conformational changes that go beyond simple two-state unfolding. Exploiting this finding, we report the first high-resolution structural models of the urea denaturation process of an alpha-helical membrane-associated protein and its completely unfolded state, which contains almost no regular secondary structure but nevertheless retains a topology close to that of the folded state.

Impact Factor

Scopus SNIP

Web of Science
Times Cited

Scopus
Cited By

Altmetric

10.677

2.351