To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

To gate or not to gate : using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations. / Khandelia, Himanshu; Jensen, Morten O.; Mouritsen, Ole G.

In: Journal of Physical Chemistry B, Vol. 113, No. 15, 16.04.2009, p. 5239-5244.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Khandelia, H, Jensen, MO & Mouritsen, OG 2009, 'To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations', Journal of Physical Chemistry B, vol. 113, no. 15, pp. 5239-5244. https://doi.org/10.1021/jp809152c

APA

Khandelia, H., Jensen, M. O., & Mouritsen, O. G. (2009). To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations. Journal of Physical Chemistry B, 113(15), 5239-5244. https://doi.org/10.1021/jp809152c

Vancouver

Khandelia H, Jensen MO, Mouritsen OG. To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations. Journal of Physical Chemistry B. 2009 Apr 16;113(15):5239-5244. https://doi.org/10.1021/jp809152c

Author

Khandelia, Himanshu ; Jensen, Morten O. ; Mouritsen, Ole G. / To gate or not to gate : using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations. In: Journal of Physical Chemistry B. 2009 ; Vol. 113, No. 15. pp. 5239-5244.

Bibtex

@article{5cf47c07229042609e77cbb8f3608115,
title = "To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations",
abstract = "The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.",
author = "Himanshu Khandelia and Jensen, {Morten O.} and Mouritsen, {Ole G.}",
year = "2009",
month = apr,
day = "16",
doi = "10.1021/jp809152c",
language = "English",
volume = "113",
pages = "5239--5244",
journal = "Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "15",

}

RIS

TY - JOUR

T1 - To gate or not to gate

T2 - using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

AU - Khandelia, Himanshu

AU - Jensen, Morten O.

AU - Mouritsen, Ole G.

PY - 2009/4/16

Y1 - 2009/4/16

N2 - The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.

AB - The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.

UR - http://www.scopus.com/inward/record.url?scp=65249172514&partnerID=8YFLogxK

U2 - 10.1021/jp809152c

DO - 10.1021/jp809152c

M3 - Journal article

AN - SCOPUS:65249172514

VL - 113

SP - 5239

EP - 5244

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

SN - 1520-6106

IS - 15

ER -

ID: 230977172