The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.
about
Kinetics of peptide folding in lipid membranesImportance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Conformation of gramicidin A in Triton X-100 micelles from CD and FTIR data: a clean example of antiparallel double β5.6 helix formation.Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.Exchange of Gramicidin between Lipid Bilayers: Implications for the Mechanism of Channel Formation.
P2860
The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.
description
2011 nî lūn-bûn
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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name
The membrane interface dictate ...... ings in gramicidin A channels.
@en
type
label
The membrane interface dictate ...... ings in gramicidin A channels.
@en
prefLabel
The membrane interface dictate ...... ings in gramicidin A channels.
@en
P2093
P2860
P356
P1433
P1476
The membrane interface dictate ...... ings in gramicidin A channels.
@en
P2093
Denise V Greathouse
Jung H Kim
Olaf S Andersen
Roger E Koeppe
P2860
P304
P356
10.1021/BI200136E
P407
P577
2011-05-13T00:00:00Z