about
Structure and function of the FeoB G-domain from Methanococcus jannaschiiCorrelation between the OmpG secondary structure and its pH-dependent alterations monitored by FTIRStructural basis of Na(+)-independent and cooperative substrate/product antiport in CaiTStructure of Human Na+/H+ Exchanger NHE1 Regulatory Region in Complex with Calmodulin and Ca2+Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationPurification, Refolding, and Crystallization of the Outer Membrane Protein OmpG from Escherichia coli.One β hairpin follows the other: exploring refolding pathways and kinetics of the transmembrane β-barrel protein OmpG.Dual energy landscape: the functional state of the β-barrel outer membrane protein G molds its unfolding energy landscape.pH-dependent interactions guide the folding and gate the transmembrane pore of the beta-barrel membrane protein OmpG.pH-induced conformational change of the beta-barrel-forming protein OmpG reconstituted into native E. coli lipids.One beta hairpin after the other: exploring mechanical unfolding pathways of the transmembrane beta-barrel protein OmpG.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
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հետազոտող
@hy
name
Stefan Köster
@ast
Stefan Köster
@en
Stefan Köster
@es
Stefan Köster
@nl
Stefan Köster
@sl
type
label
Stefan Köster
@ast
Stefan Köster
@en
Stefan Köster
@es
Stefan Köster
@nl
Stefan Köster
@sl
prefLabel
Stefan Köster
@ast
Stefan Köster
@en
Stefan Köster
@es
Stefan Köster
@nl
Stefan Köster
@sl