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A microscopic view of the mechanisms of active transport across the cellular membrane

Tutkimustuotosvertaisarvioitu

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A microscopic view of the mechanisms of active transport across the cellular membrane. / Enkavi, Giray; Li, Jing; Wen, Pochao; Thangapandian, Sundarapandian; Moradi, Mahmoud; Jiang, Tao; Han, Wei; Tajkhorshid, Emad.

julkaisussa: Annual Reports in Computational Chemistry, Vuosikerta 10, 2014, s. 77-125.

Tutkimustuotosvertaisarvioitu

Harvard

Enkavi, G, Li, J, Wen, P, Thangapandian, S, Moradi, M, Jiang, T, Han, W & Tajkhorshid, E 2014, 'A microscopic view of the mechanisms of active transport across the cellular membrane', Annual Reports in Computational Chemistry, Vuosikerta. 10, Sivut 77-125. https://doi.org/10.1016/B978-0-444-63378-1.00004-5

APA

Enkavi, G., Li, J., Wen, P., Thangapandian, S., Moradi, M., Jiang, T., ... Tajkhorshid, E. (2014). A microscopic view of the mechanisms of active transport across the cellular membrane. Annual Reports in Computational Chemistry, 10, 77-125. https://doi.org/10.1016/B978-0-444-63378-1.00004-5

Vancouver

Enkavi G, Li J, Wen P, Thangapandian S, Moradi M, Jiang T et al. A microscopic view of the mechanisms of active transport across the cellular membrane. Annual Reports in Computational Chemistry. 2014;10:77-125. https://doi.org/10.1016/B978-0-444-63378-1.00004-5

Author

Enkavi, Giray ; Li, Jing ; Wen, Pochao ; Thangapandian, Sundarapandian ; Moradi, Mahmoud ; Jiang, Tao ; Han, Wei ; Tajkhorshid, Emad. / A microscopic view of the mechanisms of active transport across the cellular membrane. Julkaisussa: Annual Reports in Computational Chemistry. 2014 ; Vuosikerta 10. Sivut 77-125.

Bibtex - Lataa

@article{68af18a47c574a7980e16b12f28c50c9,
title = "A microscopic view of the mechanisms of active transport across the cellular membrane",
abstract = "Membrane transporters are molecular machines that couple active transport of their specific substrates to various sources of cellular energy through a set of highly coordinated protein conformational changes. The alternating-access mechanism of transport in these proteins, which ensures that the substrate is only accessible from one side of the membrane at any given time, relies on complex and global protein conformational changes that are also closely coupled to molecular events such as substrate binding and translocation. In this review, we describe the application of advanced molecular modeling and simulation technologies to a number of membrane transport proteins studied in our laboratory. The goal is to demonstrate the power of the methods in describing functionally relevant molecular events ranging from more localized events such as substrate binding and gating motions to large, global protein conformational changes governing the transition of the protein between major functional states.",
keywords = "Conformational changes, Membrane transporters, Molecular dynamics, Nonequilibrium simulation, Primary transporters, Secondary transporters, Substrate binding",
author = "Giray Enkavi and Jing Li and Pochao Wen and Sundarapandian Thangapandian and Mahmoud Moradi and Tao Jiang and Wei Han and Emad Tajkhorshid",
year = "2014",
doi = "10.1016/B978-0-444-63378-1.00004-5",
language = "English",
volume = "10",
pages = "77--125",
journal = "Annual Reports in Computational Chemistry",
issn = "1574-1400",
publisher = "Elsevier BV",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - A microscopic view of the mechanisms of active transport across the cellular membrane

AU - Enkavi, Giray

AU - Li, Jing

AU - Wen, Pochao

AU - Thangapandian, Sundarapandian

AU - Moradi, Mahmoud

AU - Jiang, Tao

AU - Han, Wei

AU - Tajkhorshid, Emad

PY - 2014

Y1 - 2014

N2 - Membrane transporters are molecular machines that couple active transport of their specific substrates to various sources of cellular energy through a set of highly coordinated protein conformational changes. The alternating-access mechanism of transport in these proteins, which ensures that the substrate is only accessible from one side of the membrane at any given time, relies on complex and global protein conformational changes that are also closely coupled to molecular events such as substrate binding and translocation. In this review, we describe the application of advanced molecular modeling and simulation technologies to a number of membrane transport proteins studied in our laboratory. The goal is to demonstrate the power of the methods in describing functionally relevant molecular events ranging from more localized events such as substrate binding and gating motions to large, global protein conformational changes governing the transition of the protein between major functional states.

AB - Membrane transporters are molecular machines that couple active transport of their specific substrates to various sources of cellular energy through a set of highly coordinated protein conformational changes. The alternating-access mechanism of transport in these proteins, which ensures that the substrate is only accessible from one side of the membrane at any given time, relies on complex and global protein conformational changes that are also closely coupled to molecular events such as substrate binding and translocation. In this review, we describe the application of advanced molecular modeling and simulation technologies to a number of membrane transport proteins studied in our laboratory. The goal is to demonstrate the power of the methods in describing functionally relevant molecular events ranging from more localized events such as substrate binding and gating motions to large, global protein conformational changes governing the transition of the protein between major functional states.

KW - Conformational changes

KW - Membrane transporters

KW - Molecular dynamics

KW - Nonequilibrium simulation

KW - Primary transporters

KW - Secondary transporters

KW - Substrate binding

UR - http://www.scopus.com/inward/record.url?scp=84919386963&partnerID=8YFLogxK

U2 - 10.1016/B978-0-444-63378-1.00004-5

DO - 10.1016/B978-0-444-63378-1.00004-5

M3 - Article

VL - 10

SP - 77

EP - 125

JO - Annual Reports in Computational Chemistry

JF - Annual Reports in Computational Chemistry

SN - 1574-1400

ER -