Free energetics of arginine permeation into model DMPC lipid bilayers: coupling of effective counterion concentration and lateral bilayer dimensions (Q34447999)

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English	Free energetics of arginine permeation into model DMPC lipid bilayers: coupling of effective counterion concentration and lateral bilayer dimensions	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Free energetics of arginine permeation into model DMPC lipid bilayers: coupling of effective counterion concentration and lateral bilayer dimensions (English)

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Europe PubMed Central

PubMed publication ID

2 August 2017

author name string

Yuan Hu

1

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Europe PubMed Central

PubMed publication ID

2 August 2017

Shuching Ou

2

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Europe PubMed Central

PubMed publication ID

2 August 2017

Sandeep Patel

3

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Europe PubMed Central

PubMed publication ID

2 August 2017

language of work or name

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publication date

16 September 2013

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Europe PubMed Central

PubMed publication ID

2 August 2017

Journal of Physical Chemistry B

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Europe PubMed Central

PubMed publication ID

2 August 2017

117

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Europe PubMed Central

PubMed publication ID

2 August 2017

39

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Europe PubMed Central

PubMed publication ID

2 August 2017

11641-11653

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables.

1 reference

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6 July 2018

All-atom empirical potential for molecular modeling and dynamics studies of proteins

1 reference

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6 July 2018

Free energy of translocating an arginine-rich cell-penetrating peptide across a lipid bilayer suggests pore formation

1 reference

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6 July 2018

Exact Relation between Potential of Mean Force and Free-Energy Profile

1 reference

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6 July 2018

Membrane bending is critical for the stability of voltage sensor segments in the membrane

1 reference

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6 July 2018

Mechanism of voltage gating in potassium channels

1 reference

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A protein transduction method using oligo-arginine (3R) for the delivery of transcription factors into cell nuclei.

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Determination of membrane-insertion free energies by molecular dynamics simulations

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Arginine residues at internal positions in a protein are always charged

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The role of membrane thickness in charged protein-lipid interactions.

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Backbone rigidity and static presentation of guanidinium groups increases cellular uptake of arginine-rich cell-penetrating peptides

1 reference

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Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers

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Spontaneous membrane-translocating peptides by orthogonal high-throughput screening

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Arginine in membranes: the connection between molecular dynamics simulations and translocon-mediated insertion experiments

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6 July 2018

A look at arginine in membranes

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Defect-mediated trafficking across cell membranes: insights from in silico modeling

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Electrostatics of deformable lipid membranes

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Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types

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6 July 2018

Arginine-rich cell-penetrating peptides.

1 reference

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6 July 2018

Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides

1 reference

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6 July 2018

Cell penetrating peptides: how do they do it?

1 reference

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6 July 2018

Cell entry of arginine-rich peptides is independent of endocytosis

1 reference

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Assessing atomistic and coarse-grained force fields for protein-lipid interactions: the formidable challenge of an ionizable side chain in a membrane.

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Cell-penetrating peptides as delivery vehicles for biology and medicine

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A continuum method for determining membrane protein insertion energies and the problem of charged residues

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Cell-penetrating and cell-targeting peptides in drug delivery

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Molecular dynamics simulations of asymmetric NaCl and KCl solutions separated by phosphatidylcholine bilayers: potential drops and structural changes induced by strong Na+-lipid interactions and finite size effects

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Distribution of amino acids in a lipid bilayer from computer simulations.

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Does arginine remain protonated in the lipid membrane? Insights from microscopic pKa calculations

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Partitioning of amino acid side chains into lipid bilayers: results from computer simulations and comparison to experiment

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On the thermodynamic stability of a charged arginine side chain in a transmembrane helix

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Oligoarginine vectors for intracellular delivery: design and cellular-uptake mechanisms

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Arginine-rich cell penetrating peptides: from endosomal uptake to nuclear delivery

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Scalable molecular dynamics with NAMD

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Interface connections of a transmembrane voltage sensor

1 reference

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Recognition of transmembrane helices by the endoplasmic reticulum translocon.

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The open pore conformation of potassium channels

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VMD: visual molecular dynamics

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Transfer of arginine into lipid bilayers is nonadditive.

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Identifiers

10.1021/JP404829Y

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Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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