Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis.
about
Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micellesThymosin α1 inserts N terminus into model membranes assuming a helical conformationThe conformation of a signal peptide bound by Escherichia coli preprotein translocase SecACo-translational localization of an LTR-retrotransposon RNA to the endoplasmic reticulum nucleates virus-like particle assembly sitesPrinciples of protein folding--a perspective from simple exact models.Structure and dynamic properties of membrane proteins using NMR.Use of synthetic signal sequences to explore the protein export machinery.Protein targeting to the bacterial cytoplasmic membrane.Peptide structural analysis by solid-state NMR spectroscopy.Role of lipids in the translocation of proteins across membranes.Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB proteinEffect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence.Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy.Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formationSignal recognition particle: an essential protein-targeting machine.Fidelity of cotranslational protein targeting by the signal recognition particle.Structural Elucidation of the Cell-Penetrating Penetratin Peptide in Model Membranes at the Atomic Level: Probing Hydrophobic Interactions in the Blood-Brain BarrierAnionic phospholipids and protein translocation.Using a low denaturant model to explore the conformational features of translocation-active SecA.Genome-wide analysis of signal peptide functionality in Lactobacillus plantarum WCFS1.The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli.Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.Delta mu H+ dependency of in vitro protein translocation into Escherichia coli inner-membrane vesicles varies with the signal-sequence core-region composition.
P2860
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P2860
Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@ast
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@en
type
label
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@ast
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@en
prefLabel
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@ast
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@en
P2093
P356
P1433
P1476
Membrane-bound conformation of ...... ar Overhauser effect analysis.
@en
P2093
P304
13991-13999
P356
10.1021/BI00213A032
P407
P577
1993-12-01T00:00:00Z