Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
about
Obstructing toxin pathways by targeted pore blockageSemisynthetic Nanoreactor for Reversible Single-Molecule Covalent ChemistryOccK channels from Pseudomonas aeruginosa exhibit diverse single-channel electrical signatures but conserved anion selectivityAnalysis of gating transitions among the three major open states of the OpdK channel.Redesign of a plugged beta-barrel membrane protein.Impact of distant charge reversals within a robust beta-barrel protein poreInteractions of peptides with a protein pore.Partitioning of individual flexible polymers into a nanoscopic protein pore.Single-molecule mass spectrometry in solution using a solitary nanoporeTheory for polymer analysis using nanopore-based single-molecule mass spectrometryPolymer partitioning and ion selectivity suggest asymmetrical shape for the membrane pore formed by epsilon toxin.Single-molecule observation of protein adsorption onto an inorganic surface.Wide nanoscopic pore of maxi-anion channel suits its function as an ATP-conductive pathway.Facilitated translocation of polypeptides through a single nanopore.Applications of biological pores in nanomedicine, sensing, and nanoelectronicsSemisynthetic protein nanoreactor for single-molecule chemistryInspection of the engineered FhuA ΔC/Δ4L protein nanopore by polymer exclusion.Theory of polymer-nanopore interactions refined using molecular dynamics simulations.Protein sensing with engineered protein nanoporesReading polymers: sequencing of natural and synthetic macromolecules.Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion.Mechanism of KCl enhancement in detection of nonionic polymers by nanopore sensors.Quantitative characterization of the lipid encapsulation of quantum dots for biomedical applicationsUni-molecular detection and quantification of selected β-lactam antibiotics with a hybrid α-hemolysin protein pore.Computer simulations of the translocation and unfolding of a protein pulled mechanically through a pore.Bioorthogonal Cycloadditions with Sub-Millisecond Intermediates.Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Electric-field-driven polymer entry into asymmetric nanoscale channels.Direct force measurement of single DNA-peptide interactions using atomic force microscopy.Polymer reversal rate calculated via locally scaled diffusion map.The rate constant of polymer reversal inside a pore.Driven polymer transport through a nanopore controlled by a rotating electric field: off-lattice computer simulations.DNA in nanopores: counterion condensation and coion depletion.“Lesen” von Polymeren: Die Sequenzierung natürlicher und synthetischer MakromolekülePeptide translocation through the mesoscopic channel: binding kinetics at the single molecule level
P2860
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P2860
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@ast
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@en
type
label
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@ast
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@en
prefLabel
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@ast
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law.
@en
P2860
P356
P1476
Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
@en
P2093
Movileanu L
P2860
P304
10137-10141
P356
10.1073/PNAS.181089798
P407
P50
P577
2001-08-14T00:00:00Z