Molecular dynamics of acetylcholinesterase

Tongye Shen; Kaihsu Tai; Richard H. Henchman; J. Andrew McCammon

doi:10.1021/ar010025i

Molecular dynamics of acetylcholinesterase

Tongye Shen, Kaihsu Tai, Richard H. Henchman, J. Andrew McCammon

Research output: Contribution to journal › Article › peer-review

Abstract

Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes of regulation of the activity of the enzyme.

Original language	English
Pages (from-to)	332-340
Number of pages	8
Journal	Accounts of Chemical Research
Volume	35
Issue number	6
DOIs	https://doi.org/10.1021/ar010025i
Publication status	Published - 2002

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@article{2b160c17513640c7baeb1ce56a99f88b,

title = "Molecular dynamics of acetylcholinesterase",

abstract = "Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes of regulation of the activity of the enzyme.",

author = "Tongye Shen and Kaihsu Tai and Henchman, {Richard H.} and McCammon, {J. Andrew}",

year = "2002",

doi = "10.1021/ar010025i",

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journal = "Accounts of Chemical Research",

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publisher = "American Chemical Society",

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T1 - Molecular dynamics of acetylcholinesterase

AU - Shen, Tongye

AU - Tai, Kaihsu

AU - Henchman, Richard H.

AU - McCammon, J. Andrew

PY - 2002

Y1 - 2002

N2 - Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes of regulation of the activity of the enzyme.

AB - Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes of regulation of the activity of the enzyme.

U2 - 10.1021/ar010025i

DO - 10.1021/ar010025i

M3 - Article

SN - 0001-4842

VL - 35

SP - 332

EP - 340

JO - Accounts of Chemical Research

JF - Accounts of Chemical Research

IS - 6

ER -

Molecular dynamics of acetylcholinesterase

Abstract

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