Why ice-binding type I antifreeze protein acts as a gas hydrate crystal inhibitor

2015 ◽  
Vol 17 (15) ◽  
pp. 9984-9990 ◽  
Author(s):  
S. Alireza Bagherzadeh ◽  
Saman Alavi ◽  
John A. Ripmeester ◽  
Peter Englezos
Keyword(s):  
Gas Hydrate ◽  
Antifreeze Protein ◽  
Winter Flounder ◽  
Methyl Groups ◽  
Type I ◽  
Cooperative Action ◽  
Ice Binding ◽  
Hydrate Crystal ◽  
Binding Type

The winter flounder antifreeze protein (wf-AFP) acts as a gas hydrate crystal inhibitor by binding to the empty-half cages at the hydrate surfaceviathe cooperative action between methyl groups of threonine and alanine residues.

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.

scholarly journals Ice-binding structure and mechanism of an antifreeze protein from winter flounder

Nature ◽  
1995 ◽  
Vol 375 (6530) ◽  
pp. 427-431 ◽  
Author(s):  
F. Sicheri ◽  
D. S. C. Yang
Keyword(s):  
Antifreeze Protein ◽  
Winter Flounder ◽  
Ice Binding ◽  
Binding Structure

The inhibition of tetrahydrofuran clathrate-hydrate formation with antifreeze protein

2003 ◽  
Vol 81 (1-2) ◽  
pp. 17-24 ◽  
Author(s):  
H Zeng ◽  
L D Wilson ◽  
V K Walker ◽  
J A Ripmeester
Keyword(s):  
Induction Time ◽  
Crystal Morphology ◽  
Choristoneura Fumiferana ◽  
Hydrate Formation ◽  
Antifreeze Protein ◽  
Clathrate Hydrate ◽  
Inhibition Mechanism ◽  
Type I ◽  
Inhibition Activity ◽  
Hydrate Crystal

The effect of Type I fish antifreeze protein (AFP) from the winter flounder, Pleuronectes americanus (Walbaum), (WfAFP) on the formation of tetrahydrofuran (THF) clathrate hydrate was studied by observing changes in THF crystal morphology and determining the induction time for nucleation. AFP retarded THF clathrate-hydrate growth at the tested temperatures and modified the THF clathrate-hydrate crystal morphology from octahedral to plate-like. AFP appears to be even more effective than the kinetic inhibitor, polyvinylpyrrolidone (PVP). Recombinant AFP from an insect, a spruce budworm, Choristoneura fumiferana (Clem.), moth, (Cf) was also tested for inhibition activity by observation of the THF-hydrate-crystal-growth habit. Like WfAFP, CfAFP appeared to show adsorption on multiple THF-hydrate-crystal faces. A protein with no antifreeze activity, cytochrome C, was used as a control and it neither changed the morphology of the THF clathrate-hydrate crystals, nor retarded the formation of the hydrate. Preliminary experiments on the inhibition activity of WfAFP on a natural gas hydrate assessed induction time and the amount of propane gas consumed. Similar to the observations for THF, the data indicated that WfAFP inhibited propane-hydrate growth. Taken together, these results support our hypothesis that AFPs can inhibit clathrate-hydrate growth and as well, offer promise for the understanding of the inhibition mechanism. PACS No.: 87.90ty

scholarly journals The effect of hydrophobic analogues of the type I winter flounder antifreeze protein on lipid bilayers

FEBS Letters ◽  
2003 ◽  
Vol 551 (1-3) ◽  
pp. 13-19 ◽  
Author(s):  
Melanie M. Tomczak ◽  
Dirk K. Hincha ◽  
John H. Crowe ◽  
Margaret M. Harding ◽  
A.D.J. Haymet
Keyword(s):  
Lipid Bilayers ◽  
Antifreeze Protein ◽  
Winter Flounder ◽  
Type I

Tissue distribution of fish antifreeze protein mRNAs

1992 ◽  
Vol 70 (4) ◽  
pp. 810-814 ◽  
Author(s):  
Zhiyuan Gong ◽  
Garth L. Fletcher ◽  
Choy L. Hew
Keyword(s):  
Northern Blot Analysis ◽  
Antifreeze Protein ◽  
The Body ◽  
Winter Flounder ◽  
Type I ◽  
Pseudopleuronectes Americanus ◽  
Sea Raven ◽  
Hemitripterus Americanus ◽  
Afp Mrna ◽  
Distribution Of Fish

The presence of fish antifreeze protein (AFP) mRNA was examined in a variety of tissues from the winter flounder (Pseudopleuronectes americanus), sea raven (Hemitripterus americanus), and ocean pout (Macrozoarces americanus), each of which contains one of the three known AFP types. Northern blot analysis indicates that whereas the AFP mRNA is restricted to liver in sea raven (type II AFP), significant amounts of mRNA are present in many other tissues in both winter flounder (type I) and ocean pout (type III). These results indicate that in sea raven, antifreeze protein synthesis only occurs in the liver, whereas in the ocean pout and winter flounder, synthesis occurs in many tissues throughout the body. These investigations are relevant to understanding the mode of action of these polypeptides.

scholarly journals A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze

1996 ◽  
Vol 5 (6) ◽  
pp. 1150-1156 ◽  
Author(s):  
Heman Chao ◽  
Robert S. Hodges ◽  
Cyril M. Kay ◽  
Sherry Y. Gauthier ◽  
Peter L. Davies
Keyword(s):  
Antifreeze Protein ◽  
Type I ◽  
Ice Binding ◽  
Natural Variant

Alternative Roles for Putative Ice-Binding Residues in Type I Antifreeze Protein†

Biochemistry ◽  
1999 ◽  
Vol 38 (15) ◽  
pp. 4743-4749 ◽  
Author(s):  
Michèle C. Loewen ◽  
Heman Chao ◽  
Michael E. Houston, ◽  
Jason Baardsnes ◽  
Robert S. Hodges ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Type I ◽  
Ice Binding ◽  
Binding Residues

Temperature-dependent Kinetics Study for Hydrogen Exchange of Type I Antifreeze Protein from Winter Flounder

2014 ◽  
Vol 35 (1) ◽  
pp. 286-288
Author(s):  
Hee-Eun Kim ◽  
Minjee Jeong ◽  
Ae-Ree Lee ◽  
Chin-Ju Park ◽  
Joon-Hwa Lee
Keyword(s):  
Hydrogen Exchange ◽  
Antifreeze Protein ◽  
Winter Flounder ◽  
Type I ◽  
Kinetics Study ◽  
Temperature Dependent
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