The ice/water interface: Molecular dynamics simulations of the basal, prism, {202̄1}, and {21̄1̄0} interfaces of ice Ih

Hayward, Jennifer A.; Haymet, A. D. J.

doi:10.1063/1.1333680

Cited by 97 publications

(103 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, our recent studies have shown that there is significant charge inhomogeneity at the ice/water interface (54,55). The full charge distribution of SS3, or any polypeptide, interacts with the charge inhomogeneity that occurs naturally at any broad interface such as the ice/water interface.…”

Section: Discussionmentioning

confidence: 99%

Type I Shorthorn Sculpin Antifreeze Protein

Fairley¹,

Westman²,

Pham³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

A number of structurally diverse classes of "antifreeze" proteins that allow fish to survive in sub-zero ice-laden waters have been isolated from the blood plasma of cold water teleosts. However, despite receiving a great deal of attention, the one or more mechanisms through which these proteins act are not fully understood. In this report we have synthesized a type I antifreeze polypeptide (AFP) from the shorthorn sculpin Myoxocephalus scorpius using recombinant methods. Construction of a synthetic gene with optimized codon usage and expression as a glutathione S-transferase fusion protein followed by purification yielded milligram amounts of polypeptide with two extra residues appended to the N terminus. Circular dichroism and NMR experiments, including residual dipolar coupling measurements on a 15 N-labeled recombinant polypeptide, show that the polypeptides are ␣-helical with the first four residues being more flexible than the remainder of the sequence. Both the recombinant and synthetic polypeptides modify ice growth, forming facetted crystals just below the freezing point, but display negligible thermal hysteresis. Acetylation of Lys-10, Lys-20, and Lys-21 as well as the N terminus of the recombinant polypeptide gave a derivative that displays both thermal hysteresis (0.4°C at 15 mg/ml) and ice crystal faceting. These results confirm that the N terminus of wild-type polypeptide is functionally important and support our previously proposed mechanism for all type I proteins, in which the hydrophobic face is oriented toward the ice at the ice/water interface.The type I AFPs 1 found in the blood of cold water teleosts (1-3) have attracted significant interest, due to the potential applications of such compounds in biotechnology and medicine (4 -9). These compounds are alanine-rich ␣-helical proteins of 33-47 residues in length (for reviews see Refs. 10 -13). Although 14 type I proteins have been identified in nature (summarized in Ref. 12), almost all studies to date have centered on HPLC6, the 37-residue protein from the winter flounder (see Table I below) (14). This protein is characterized as an AFP, because it modifies both the rate and shape of ice crystal growth and displays thermal hysteresis, i.e. a positive difference between the ice growth temperature and the equilibrium melting temperature of ice.During the last decade, significant progress has been made in elucidating the structural features of HPLC6 that are required to give antifreeze activity. Structure-activity studies have identified the importance of the Thr residues at positions 2, 13, 24, and 35 plus surrounding residues, for ice growth inhibition activity. Although the Thr residues were assumed to be involved in hydrogen-bonding interactions with ice for many years (15-19), more recent mutations have identified the hydrophobicity provided by the ␥-methyl group of Thr as a key factor related to the ability to inhibit ice growth (20 -24). Hydrogen bonding and other roles for the surrounding residues have also been considered (24 -29). Howe...

show abstract

Section: Discussionmentioning

confidence: 99%

Type I Shorthorn Sculpin Antifreeze Protein

Fairley¹,

Westman²,

Pham³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…146 On the one hand, preconfigured icelike water molecules on the IBS would facilitate ice-binding by inducing ice growth in the interfacial region between ice and bulk water, which is intrinsically disordered and approximately 10-20 Å thick. 147 On the other hand, waters near the non-IBS would be more distorted to prevent engulfment in the ice. The authors further proposed that the high entropic gain of merging the preorganized waters at the IBS with ice through this "zipper mechanism" would sufficiently reduce the free energy of the system to result in quasi-irreversible binding.…”

Section: Dual Function Of the Hydration Layermentioning

confidence: 99%

Interaction of ice binding proteins with ice, water and ions

et al. 2016

View full text Add to dashboard Cite

Articles you may be interested inExplicit-water theory for the salt-specific effects and Hofmeister series in protein solutions J. Chem. Phys. 144, 215101 (2016) Ice binding proteins (IBPs) are produced by various cold-adapted organisms to protect their body tissues against freeze damage. First discovered in Antarctic fish living in shallow waters, IBPs were later found in insects, microorganisms, and plants. Despite great structural diversity, all IBPs adhere to growing ice crystals, which is essential for their extensive repertoire of biological functions. Some IBPs maintain liquid inclusions within ice or inhibit recrystallization of ice, while other types suppress freezing by blocking further ice growth. In contrast, ice nucleating proteins stimulate ice nucleation just below 0 C. Despite huge commercial interest and major scientific breakthroughs, the precise working mechanism of IBPs has not yet been unraveled. In this review, the authors outline the state-of-the-art in experimental and theoretical IBP research and discuss future scientific challenges. The interaction of IBPs with ice, water and ions is examined, focusing in particular on ice growth inhibition mechanisms.

show abstract

“…Although the adsorption-inhibition mechanism for ice growth inhibition has been generally accepted for Ͼ30 years, the mechanism by which AFPs recognize and bind ice has gone through several radical revisions without a consensus emerging. Recent simulations reveal that in contrast to other inorganic surfaces to which proteins may bind, an ice surface is disordered at the molecular level, with a 1-2-nm transition region separating ice from the surrounding bulk water solution (5).…”

mentioning

confidence: 99%

Crystal Structure of an Insect Antifreeze Protein and Its Implications for Ice Binding

Hakim

Nguyen

Basu

et al. 2013

Journal of Biological Chemistry

103

121

View full text Add to dashboard Cite

Background: Antifreeze proteins bind to ice crystals and inhibit their growth. Results: The crystal structure of a potent beetle antifreeze protein was determined by direct methods. Conclusion: Ordered crystallographic waters on the protein surface match several planes of hexagonal ice. Significance: The structure is the largest determined ab initio without heavy atoms, and its ordered waters suggest a molecular basis for ice binding.

show abstract

The ice/water interface: Molecular dynamics simulations of the basal, prism, {202̄1}, and {21̄1̄0} interfaces of ice Ih

Cited by 97 publications

References 76 publications

Type I Shorthorn Sculpin Antifreeze Protein

Type I Shorthorn Sculpin Antifreeze Protein

Interaction of ice binding proteins with ice, water and ions

Crystal Structure of an Insect Antifreeze Protein and Its Implications for Ice Binding

Contact Info

Product

Resources

About