High water mobility on the ice-binding surface of a hyperactive antifreeze protein.
Modig, Kristofer LU
; Qvist, Johan
LU
; Marshall, Christopher B
; Davies, Peter L
and Halle, Bertil
LU
(2010)
In Physical chemistry chemical physics : PCCP
12(Online 29th July 2010).
p.10189-10197
- Abstract
- Antifreeze proteins (AFPs) prevent uncontrolled ice formation in organisms exposed to subzero temperatures by binding irreversibly to specific planes of nascent ice crystals. To understand the thermodynamic driving forces and kinetic mechanism of AFP activity, it is necessary to characterize the hydration behavior of these proteins in solution. With this aim, we have studied the hyperactive insect AFP from Tenebrio molitor (TmAFP) with the (17)O magnetic relaxation dispersion (MRD) method, which selectively monitors the rotational motion and exchange kinetics of water molecules on picosecond-microsecond time scales. The global hydration behavior of TmAFP is found to be similar to non-antifreeze proteins, with no evidence of ice-like or... (More)
- Antifreeze proteins (AFPs) prevent uncontrolled ice formation in organisms exposed to subzero temperatures by binding irreversibly to specific planes of nascent ice crystals. To understand the thermodynamic driving forces and kinetic mechanism of AFP activity, it is necessary to characterize the hydration behavior of these proteins in solution. With this aim, we have studied the hyperactive insect AFP from Tenebrio molitor (TmAFP) with the (17)O magnetic relaxation dispersion (MRD) method, which selectively monitors the rotational motion and exchange kinetics of water molecules on picosecond-microsecond time scales. The global hydration behavior of TmAFP is found to be similar to non-antifreeze proteins, with no evidence of ice-like or long-ranged modifications of the solvent. However, two sets of structural water molecules, located within the core and on the ice-binding face in the crystal structure of TmAFP, may have functional significance. We find that 2 of the 5 internal water molecules exchange with a residence time of 8 +/- 1 mus at 300 K and a large activation energy of approximately 50 kJ mol(-1), reflecting intermittent large-scale conformational fluctuations in this exceptionally dense and rigid protein. Six water molecules arrayed with ice-like spacing in the central trough on the ice-binding face exchange with bulk water on a sub-nanosecond time scale. The combination of high order and fast exchange may allow these water molecules to contribute entropically to the ice-binding affinity without limiting the absorption rate. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1644451
- author
- Modig, Kristofer
LU
; Qvist, Johan
LU
; Marshall, Christopher B
; Davies, Peter L
and Halle, Bertil
LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Physical chemistry chemical physics : PCCP
- volume
- 12
- issue
- Online 29th July 2010
- pages
- 10189 - 10197
- publisher
- Royal Society of Chemistry
- external identifiers
-
- wos:000281352300006
- pmid:20668761
- scopus:77957999861
- pmid:20668761
- ISSN
- 1463-9084
- DOI
- 10.1039/c002970j
- language
- English
- LU publication?
- yes
- id
- 4b77371e-9a7a-42fe-93b4-7f20ce1c8d8e (old id 1644451)
- date added to LUP
- 2016-04-01 13:44:09
- date last changed
- 2022-03-06 07:28:21
@article{4b77371e-9a7a-42fe-93b4-7f20ce1c8d8e,
abstract = {{Antifreeze proteins (AFPs) prevent uncontrolled ice formation in organisms exposed to subzero temperatures by binding irreversibly to specific planes of nascent ice crystals. To understand the thermodynamic driving forces and kinetic mechanism of AFP activity, it is necessary to characterize the hydration behavior of these proteins in solution. With this aim, we have studied the hyperactive insect AFP from Tenebrio molitor (TmAFP) with the (17)O magnetic relaxation dispersion (MRD) method, which selectively monitors the rotational motion and exchange kinetics of water molecules on picosecond-microsecond time scales. The global hydration behavior of TmAFP is found to be similar to non-antifreeze proteins, with no evidence of ice-like or long-ranged modifications of the solvent. However, two sets of structural water molecules, located within the core and on the ice-binding face in the crystal structure of TmAFP, may have functional significance. We find that 2 of the 5 internal water molecules exchange with a residence time of 8 +/- 1 mus at 300 K and a large activation energy of approximately 50 kJ mol(-1), reflecting intermittent large-scale conformational fluctuations in this exceptionally dense and rigid protein. Six water molecules arrayed with ice-like spacing in the central trough on the ice-binding face exchange with bulk water on a sub-nanosecond time scale. The combination of high order and fast exchange may allow these water molecules to contribute entropically to the ice-binding affinity without limiting the absorption rate.}},
author = {{Modig, Kristofer and Qvist, Johan and Marshall, Christopher B and Davies, Peter L and Halle, Bertil}},
issn = {{1463-9084}},
language = {{eng}},
number = {{Online 29th July 2010}},
pages = {{10189--10197}},
publisher = {{Royal Society of Chemistry}},
series = {{Physical chemistry chemical physics : PCCP}},
title = {{High water mobility on the ice-binding surface of a hyperactive antifreeze protein.}},
url = {{http://dx.doi.org/10.1039/c002970j}},
doi = {{10.1039/c002970j}},
volume = {{12}},
year = {{2010}},
}