Perturbation of long-range water dynamics as the mechanism for the antifreeze activity of antifreeze glycoprotein

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dc.contributor.author Mallajosyula, Sairam Swaroop
dc.contributor.author Vanommeslaeghe, Kenno
dc.contributor.author MacKerell, Alexander D.
dc.date.accessioned 2014-08-28T11:29:45Z
dc.date.available 2014-08-28T11:29:45Z
dc.date.issued 2014-08
dc.identifier.citation Mallajosyula, Sairam S.;Vanommeslaeghe, Kenno and MacKerell, Alexander D., “Perturbation of long-range water dynamics as the mechanism for the antifreeze activity of antifreeze glycoprotein”, The Journal of Physical Chemistry, DOI: 10.1021/jp508128d, Aug. 2014 en_US
dc.identifier.issn 1520-6106
dc.identifier.uri http://dx.doi.org/10.1021/jp508128d
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/1380
dc.description.abstract Very little is known about the mechanism of antifreeze action of antifreeze glycoproteins (AFGPs) present in Antarctic teleost fish. Recent NMR and CD studies assisted with total synthesis of synthetic AFGP variants have provided insight into the structure of short AFGP glycopeptides, though the observations did not yield information on the antifreeze mechanism of action. In this study, we use Hamiltonian replica exchange (HREX) molecular dynamics simulations to probe the structure and surrounding aqueous environments of both the natural (AFGP8) and synthetic (s-AFGP4) AFGPs. AFGPs can adopt both amphiphilic and pseudoamphiphilic conformations, the preference of which is related to the proline content of the peptide. The arrangement of carbohydrates allows the hydroxyl groups on terminal galactose units to form stable water bridges which in turn influence the hydrogen-bond network, structure, and dynamics of the surrounding solvent. Interestingly, these local effects lead to the perturbation of the tetrahedral environment for water molecules in hydration layers far (10.0–12.0 Å) from the AFGPs. This structure-induced alteration of long-range hydration dynamics is proposed to be the major contributor to antifreeze activity, a conclusion that is in line with terahertz spectroscopy experiments. The detailed structure–mechanism correlation provided in this study could lead to the design of better synthetic AFGP variants. en_US
dc.description.statementofresponsibility by Sairam S. Mallajosyula, Kenno Vanommeslaeghe and Alexander D. MacKerell
dc.format.extent vol. 118, no. 40, pp. 11696-11706
dc.language.iso en en_US
dc.publisher ACS Publication en_US
dc.subject AFGP variants en_US
dc.subject Amphiphilic en_US
dc.subject Antifreeze glycoproteins en_US
dc.subject Molecular dynamics en_US
dc.title Perturbation of long-range water dynamics as the mechanism for the antifreeze activity of antifreeze glycoprotein en_US
dc.type Article en_US
dc.relation.journal The Journal of Physical Chemistry


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