scholarly journals A peek at ice binding by antifreeze proteins

2011 ◽  
Vol 108 (18) ◽  
pp. 7281-7282 ◽  
Author(s):  
K. A. Sharp
2016 ◽  
Vol 113 (51) ◽  
pp. 14739-14744 ◽  
Author(s):  
Kai Liu ◽  
Chunlei Wang ◽  
Ji Ma ◽  
Guosheng Shi ◽  
Xi Yao ◽  
...  

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.


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

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 ◽  
...  

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

2018 ◽  
Vol 20 (42) ◽  
pp. 26926-26933 ◽  
Author(s):  
Dominique Verreault ◽  
Sarah Alamdari ◽  
Steven J. Roeters ◽  
Ravindra Pandey ◽  
Jim Pfaendtner ◽  
...  

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.


Author(s):  
Koli Basu ◽  
Christopher P. Garnham ◽  
Yoshiyuki Nishimiya ◽  
Sakae Tsuda ◽  
Ido Braslavsky ◽  
...  

2003 ◽  
Vol 81 (1-2) ◽  
pp. 39-45 ◽  
Author(s):  
B Wathen ◽  
M J Kuiper ◽  
V K Walker ◽  
Z Jia

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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