Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein

Yossi Tsfadia; Ran Friedman; Jonathan Kadmon; Anna Selzer; Esther Nachliel; Menachem Gutman

doi:10.1016/j.febslet.2007.02.033

Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein

Yossi Tsfadia^*, Ran Friedman, Jonathan Kadmon, Anna Selzer, Esther Nachliel, Menachem Gutman

^*Corresponding author for this work

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

37 Scopus citations

Abstract

The entry of substrate into the active site is the first event in any enzymatic reaction. However, due to the short time interval between the encounter and the formation of the stable complex, the detailed steps are experimentally unobserved. In the present study, we report a molecular dynamics simulation of the encounter between palmitate molecule and the Toad Liver fatty acid binding protein, ending with the formation of a stable complex resemblance in structure of other proteins of this family. The forces operating on the system leading to the formation of the tight complex are discussed.

Original language	English
Pages (from-to)	1243-1247
Number of pages	5
Journal	FEBS Letters
Volume	581
Issue number	6
DOIs	https://doi.org/10.1016/j.febslet.2007.02.033
State	Published - 20 Mar 2007
Externally published	Yes

Bibliographical note

Funding Information:
This study was supported by the United States–Israel Binational Science Foundation (2002129). R.F. greatly acknowledges the Colton Foundation for supporting him through the Colton Fellowship.

Keywords

Fatty acid binding proteins
Molecular dynamics
Molecular modeling
Palmitic acid

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10.1016/j.febslet.2007.02.033

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abstract = "The entry of substrate into the active site is the first event in any enzymatic reaction. However, due to the short time interval between the encounter and the formation of the stable complex, the detailed steps are experimentally unobserved. In the present study, we report a molecular dynamics simulation of the encounter between palmitate molecule and the Toad Liver fatty acid binding protein, ending with the formation of a stable complex resemblance in structure of other proteins of this family. The forces operating on the system leading to the formation of the tight complex are discussed.",

keywords = "Fatty acid binding proteins, Molecular dynamics, Molecular modeling, Palmitic acid",

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AU - Friedman, Ran

AU - Kadmon, Jonathan

AU - Selzer, Anna

AU - Nachliel, Esther

AU - Gutman, Menachem

N1 - Funding Information: This study was supported by the United States–Israel Binational Science Foundation (2002129). R.F. greatly acknowledges the Colton Foundation for supporting him through the Colton Fellowship.

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AB - The entry of substrate into the active site is the first event in any enzymatic reaction. However, due to the short time interval between the encounter and the formation of the stable complex, the detailed steps are experimentally unobserved. In the present study, we report a molecular dynamics simulation of the encounter between palmitate molecule and the Toad Liver fatty acid binding protein, ending with the formation of a stable complex resemblance in structure of other proteins of this family. The forces operating on the system leading to the formation of the tight complex are discussed.

KW - Fatty acid binding proteins

KW - Molecular dynamics

KW - Molecular modeling

KW - Palmitic acid

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Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein

Abstract

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Keywords

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