Why ice-binding type I antifreeze protein acts as a gas hydrate crystal inhibitor

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DOIResolve DOI: http://doi.org/10.1039/c4cp05003g
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TypeArticle
Journal titlePhysical Chemistry Chemical Physics
ISSN1463-9076
Volume17
Issue15
Pages99849990; # of pages: 7
AbstractAntifreeze proteins (AFPs) prevent ice growth by binding to a specific ice plane. Some AFPs have been found to inhibit the formation of gas hydrates which are a serious safety and operational challenge for the oil and gas industry. Molecular dynamics simulations are used to determine the mechanism of action of the winter flounder AFP (wf-AFP) in inhibiting methane hydrate growth. The wf-AFP adsorbs onto the methane hydrate surface via cooperative binding of a set of hydrophobic methyl pendant groups to the empty half-cages at the hydrate/water interface. Each binding set is composed of the methyl side chain of threonine and two alanine residues, four and seven places further down in the sequence of the protein. Understanding the principle of action of AFPs can lead to the rational design of green hydrate inhibitor molecules with potential superior performance.
Publication date
PublisherRoyal Society of Chemistry
LanguageEnglish
AffiliationNational Research Council Canada; Security and Disruptive Technologies
Peer reviewedYes
NPARC number21275722
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Record identifierb1ecb715-c382-4375-bddc-23726032b9e5
Record created2015-07-14
Record modified2016-05-09
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