scholarly journals Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

10.3791/51185 ◽  
2014 ◽  
Author(s):  
Koli Basu ◽  
Christopher P. Garnham ◽  
Yoshiyuki Nishimiya ◽  
Sakae Tsuda ◽  
Ido Braslavsky ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Ice Binding

scholarly journals Janus effect of antifreeze proteins on ice nucleation

2016 ◽  
Vol 113 (51) ◽  
pp. 14739-14744 ◽  
Author(s):  
Kai Liu ◽  
Chunlei Wang ◽  
Ji Ma ◽  
Guosheng Shi ◽  
Xi Yao ◽  
...  
Keyword(s):  
Liquid Water ◽  
Molecular Level ◽  
Simulation Analysis ◽  
Antifreeze Proteins ◽  
Freezing Temperature ◽  
Ice Nucleation ◽  
Dynamics Simulation ◽  
Ice Binding ◽  
Solid Substrates ◽  
Unique Capability

The mechanism of ice nucleation at the molecular level remains largely unknown. Nature endows antifreeze proteins (AFPs) with the unique capability of controlling ice formation. However, the effect of AFPs on ice nucleation has been under debate. Here we report the observation of both depression and promotion effects of AFPs on ice nucleation via selectively binding the ice-binding face (IBF) and the non–ice-binding face (NIBF) of AFPs to solid substrates. Freezing temperature and delay time assays show that ice nucleation is depressed with the NIBF exposed to liquid water, whereas ice nucleation is facilitated with the IBF exposed to liquid water. The generality of this Janus effect is verified by investigating three representative AFPs. Molecular dynamics simulation analysis shows that the Janus effect can be established by the distinct structures of the hydration layer around IBF and NIBF. Our work greatly enhances the understanding of the mechanism of AFPs at the molecular level and brings insights to the fundamentals of heterogeneous ice nucleation.

Hydration Shell of Antifreeze Proteins: Unveiling the Role of Non-Ice-Binding Surfaces

2019 ◽  
Vol 123 (30) ◽  
pp. 6474-6480 ◽  
Author(s):  
Laura Zanetti-Polzi ◽  
Akash Deep Biswas ◽  
Sara Del Galdo ◽  
Vincenzo Barone ◽  
Isabella Daidone
Keyword(s):  
Antifreeze Proteins ◽  
Hydration Shell ◽  
Ice Binding

Multivalent Display of Antifreeze Proteins by Fusion to Self-Assembling Protein Cages Enhances Ice-Binding Activities

Biochemistry ◽  
2016 ◽  
Vol 55 (49) ◽  
pp. 6811-6820 ◽  
Author(s):  
Sean W. Phippen ◽  
Corey A. Stevens ◽  
Tyler D. R. Vance ◽  
Neil P. King ◽  
David Baker ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Protein Cages ◽  
Self Assembling ◽  
Ice Binding ◽  
Multivalent Display

Understanding the mechanism of ice binding by type III antifreeze proteins

2001 ◽  
Vol 305 (4) ◽  
pp. 875-889 ◽  
Author(s):  
Alfred A. Antson ◽  
Derek J. Smith ◽  
David I. Roper ◽  
Sally Lewis ◽  
Leo S.D. Caves ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Type Iii ◽  
Ice Binding

scholarly journals Ice-binding site of surface-bound type III antifreeze protein partially decoupled from water

2018 ◽  
Vol 20 (42) ◽  
pp. 26926-26933 ◽  
Author(s):  
Dominique Verreault ◽  
Sarah Alamdari ◽  
Steven J. Roeters ◽  
Ravindra Pandey ◽  
Jim Pfaendtner ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Proteins ◽  
Antifreeze Protein ◽  
Water Interface ◽  
Native State ◽  
Type Iii ◽  
Ice Binding ◽  
Air Water Interface

Combined SFG/MD analysis together with spectral calculations revealed that type III antifreeze proteins adsorbed at the air–water interface maintains a native state and adopts an orientation that leads to a partial decoupling of its ice-binding site from water.

Three-dimensional simulation of ice growth in the presence of antifreeze proteins

2003 ◽  
Vol 81 (1-2) ◽  
pp. 39-45 ◽  
Author(s):  
B Wathen ◽  
M J Kuiper ◽  
V K Walker ◽  
Z Jia
Keyword(s):  
Crystal Growth ◽  
Growth Inhibition ◽  
Antifreeze Proteins ◽  
Three Dimensional ◽  
Computational Method ◽  
Inhibition Mechanism ◽  
Ice Crystal ◽  
Ice Growth ◽  
Ice Binding ◽  
Dimensional Simulation

A Monte Carlo computational method for simulating the growth of entire ice crystals from the liquid phase has been developed specifically to study the inhibition of ice-crystal growth by antifreeze proteins (AFPs). AFPs are found in the fluids of certain organisms that inhabit freezing environments and constrain ice-crystal growth by adsorbtion to the ice surface, but their inhibition mechanism is still poorly understood. Thus, it was of interest to incorporate these molecules into the dynamic ice simulations to examine the inhibition phenomenon on a whole-crystal basis. We have undertaken simulations with AFPs from two different organisms that differ in activity; the insect AFP has up to 100 times the activity of the fish AFP on a molar basis. Simulations involving insect and fish AFPs have achieved ice-growth inhibition at simulation temperatures within reported activity ranges for both fish and insect AFPs, accompanied by resulting ice morphologies similar to those observed experimentally. These results, as well as other studies on ice-etching patterns and ice burst growth at temperatures below known AFP ice-growth inhibition abilities suggest that AFP activity is dominated by the AFP ice-binding position rather than AFP ice-binding strength. PACS No.: 07.05T

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