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Solvation Layer of Antifreeze Proteins Analyzed with a Markov State Model.
- Source :
-
The journal of physical chemistry. B [J Phys Chem B] 2018 Dec 13; Vol. 122 (49), pp. 11014-11022. Date of Electronic Publication: 2018 Jun 27. - Publication Year :
- 2018
-
Abstract
- Three structurally very different antifreeze proteins (AFPs) are studied, addressing the question as to what extent the hypothesized preordering-binding mechanism is still relevant in the second solvation layer of the protein and beyond. Assuming a two-state model of water, the solvation layers are analyzed with the help of molecular dynamics simulations together with a Markov state model, which investigates the local tedrahedrality of the water hydrogen-bond network around a given water molecule. It has been shown previously that this analysis can discriminate the high-entropy, high-density state of the liquid (HDL) from its more structured low-density state (LDL). All investigated proteins, regardless of whether they are an AFP or not, have a tendency to increase the amount of HDL in their second solvation layer. The ice binding site (IBS) of the antifreeze proteins counteracts that trend, with either a hole in the HDL layer or a true excess of LDL. The results correlate to a certain extent with recent experiments, which have observed ice-like vibrational (VSFG) spectra for the water atop the IBS of only a subset of antifreeze proteins. It is concluded that the preordering-binding mechanism indeed seems to play a role but is only part of the overall picture.
Details
- Language :
- English
- ISSN :
- 1520-5207
- Volume :
- 122
- Issue :
- 49
- Database :
- MEDLINE
- Journal :
- The journal of physical chemistry. B
- Publication Type :
- Academic Journal
- Accession number :
- 29889528
- Full Text :
- https://doi.org/10.1021/acs.jpcb.8b04491