Differential Hydration of Ice‐Binding Surface of Globular and Hyperactive Antifreeze Proteins

2021 ◽  
pp. 2100090
Author(s):  
Prasun Pal ◽  
Sandipan Chakraborty ◽  
Biman Jana
Keyword(s):  
Antifreeze Proteins ◽  
Ice Binding ◽  
Binding Surface

scholarly journals Preordering of water is not needed for ice recognition by hyperactive antifreeze proteins

2018 ◽  
Vol 115 (33) ◽  
pp. 8266-8271 ◽  
Author(s):  
Arpa Hudait ◽  
Daniel R. Moberg ◽  
Yuqing Qiu ◽  
Nathan Odendahl ◽  
Francesco Paesani ◽  
...  
Keyword(s):  
Binding Site ◽  
Raman Spectra ◽  
Antifreeze Proteins ◽  
Antifreeze Protein ◽  
Bulk Liquid ◽  
Cold Environments ◽  
Ice Surface ◽  
Ice Binding ◽  
Binding Surface ◽  
Optimal Candidate

Antifreeze proteins (AFPs) inhibit ice growth in organisms living in cold environments. Hyperactive insect AFPs are particularly effective, binding ice through “anchored clathrate” motifs. It has been hypothesized that the binding of hyperactive AFPs to ice is facilitated by preordering of water at the ice-binding site (IBS) of the protein in solution. The antifreeze proteinTmAFP displays the best matching of its binding site to ice, making it the optimal candidate to develop ice-like order in solution. Here we use multiresolution simulations to unravel the mechanism by whichTmAFP recognizes and binds ice. We find that water at the IBS of the antifreeze protein in solution does not acquire ice-like or anchored clathrate-like order. Ice recognition occurs by slow diffusion of the protein to achieve the proper orientation with respect to the ice surface, followed by fast collective organization of the hydration water at the IBS to form an anchored clathrate motif that latches the protein to the ice surface. The simulations suggest that anchored clathrate order could develop on the large ice-binding surfaces of aggregates of ice-nucleating proteins (INP). We compute the infrared and Raman spectra of water in the anchored clathrate motif. The signatures of the OH stretch of water in the anchored clathrate motif can be distinguished from those of bulk liquid in the Raman spectra, but not in the infrared spectra. We thus suggest that Raman spectroscopy may be used to probe the anchored clathrate order at the ice-binding surface of INP aggregates.

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

scholarly journals A peek at ice binding by antifreeze proteins

2011 ◽  
Vol 108 (18) ◽  
pp. 7281-7282 ◽  
Author(s):  
K. A. Sharp
Keyword(s):  
Antifreeze Proteins ◽  
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

scholarly journals Ice-binding mechanism of winter flounder antifreeze proteins

1997 ◽  
Vol 73 (6) ◽  
pp. 2851-2873 ◽  
Author(s):  
A. Cheng ◽  
K.M. Merz
Keyword(s):  
Antifreeze Proteins ◽  
Winter Flounder ◽  
Binding Mechanism ◽  
Ice Binding

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 NMR Characterizations of the Ice Binding Surface of an Antifreeze Protein

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e15682 ◽  
Author(s):  
Jiang Hong ◽  
Yunfei Hu ◽  
Congmin Li ◽  
Zongchao Jia ◽  
Bin Xia ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Ice Binding ◽  
Binding Surface

Ordered hydration layer mediated ice adsorption of a globular antifreeze protein: mechanistic insight

2019 ◽  
Vol 21 (35) ◽  
pp. 19298-19310 ◽  
Author(s):  
Sandipan Chakraborty ◽  
Biman Jana
Keyword(s):  
Antifreeze Protein ◽  
Hydration Layer ◽  
Type Iii ◽  
Ice Surface ◽  
Mechanistic Insight ◽  
Ice Binding ◽  
Binding Surface ◽  
Lower Temperature

The ice binding surface of a type III AFP induces water ordering at lower temperature, which mediates its adsorption on the ice surface.

Sign in / Sign up

Export Citation Format

Share Document