scholarly journals Antifreeze protein from shorthorn sculpin: Identification of the ice-binding surface

2009 ◽  
Vol 10 (12) ◽  
pp. 2566-2576 ◽  
Author(s):  
Jason Baardsnes ◽  
Masood Jelokhani-Niaraki ◽  
Leslie H. Kondejewski ◽  
Michael J. Kuiper ◽  
Cyril M. Kay ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Ice Binding ◽  
Binding Surface ◽  
Shorthorn Sculpin

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.

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 Antifreeze Protein-induced Morphological Modification Mechanisms Linked to Ice Binding Surface

2004 ◽  
Vol 279 (31) ◽  
pp. 32407-32417 ◽  
Author(s):  
Christina S. Strom ◽  
Xiang Yang Liu ◽  
Zongchao Jia
Keyword(s):  
Antifreeze Protein ◽  
Ice Binding ◽  
Binding Surface ◽  
Morphological Modification

scholarly journals Identification of the Ice-Binding Surface on a Type III Antifreeze Protein with a “Flatness Function” Algorithm

1998 ◽  
Vol 74 (5) ◽  
pp. 2142-2151 ◽  
Author(s):  
Daniel S.C. Yang ◽  
Wai-Ching Hon ◽  
Steve Bubanko ◽  
Yiqi Xue ◽  
J. Seetharaman ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Type Iii ◽  
Ice Binding ◽  
Binding Surface

High water mobility on the ice-binding surface of a hyperactive antifreeze protein

2010 ◽  
Vol 12 (35) ◽  
pp. 10189 ◽  
Author(s):  
Kristofer Modig ◽  
Johan Qvist ◽  
Christopher B. Marshall ◽  
Peter L. Davies ◽  
Bertil Halle
Keyword(s):  
Antifreeze Protein ◽  
High Water ◽  
Water Mobility ◽  
Ice Binding ◽  
Binding Surface

Structures and ice-binding faces of the alanine-rich type I antifreeze proteinsThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

2010 ◽  
Vol 88 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Shruti N. Patel ◽  
Steffen P. Graether
Keyword(s):  
Analytical Ultracentrifugation ◽  
Peer Review Process ◽  
Winter Flounder ◽  
Type I ◽  
Ice Binding ◽  
Shorthorn Sculpin ◽  
High Resolution Structure ◽  
Dimerization Interface ◽  
Α Helix ◽  
Almost All

Antifreeze proteins (AFPs) protect cold-blooded organisms from the damage caused by freezing through their ability to inhibit ice growth. The type I AFP family, found in several fish species, contains proteins that have a high alanine content (>60% of the sequence) and structures that are almost all α-helical. We examine the structure of the type I AFP isoforms HPLC6 from winter flounder, shorthorn sculpin 3, and the winter flounder hyperactive type I AFP. The HPLC6 isoform structure consists of a single α-helix that is 37 residues long, whereas the shorthorn sculpin 3 isoform consists of two helical regions separated by a kink. The high-resolution structure of the hyperactive type I AFP has yet to be determined, but circular dichroism data and analytical ultracentrifugation suggest that the 195 residue protein is a side-by-side dimer of two α-helices. The alanine-rich ice-binding faces of HPLC6 and hyperactive type I AFP are discussed, and we propose that the ice-binding face of the shorthorn sculpin 3 AFP contains Ala14, Ala19, and Ala25. We also propose that the denaturation of hyperactive type I AFP at room temperature is explained by the stabilization of the dimerization interface through hydrogen bonds.

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