Crystallization of Water on Ferritin – Ice Nucleation by Size, Shape or Surface Chemistry?

Melillo, Jorge H.; Nikulina, Elizaveta; Bittner, Alexander M.; Cerveny, Silvina

doi:10.2139/ssrn.4405820

Cited by 2 publications

(6 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our findings from the basic structural analyses of the semi-clathrate combining both experimental and computational methods reveal critical information about the stability and construction of artificial semi-clathrate structure on a protein surface. The unique water network might be responsible for providing the interaction of ice with ferritin as reported previously. , If suitable alanine residues are placed within the confined environment, particularly at the interface of two helices, the resulting engineered protein could form a new semi-clathrate structure. Such studies are in progress.…”

Section: Discussionmentioning

confidence: 77%

“…The unique water network might be responsible for providing the interaction of ice with ferritin as reported previously. 25,26 If suitable alanine residues are placed within the confined environment, particularly at the interface of two helices, the resulting engineered protein could form a new semi-clathrate structure. Such studies are in progress.…”

Section: ■ Discussionmentioning

confidence: 99%

“…Interactions of ferritin with ice nuclei have been studied by analytical methods such as dynamic light scattering and differential scanning calorimetry. 25,26 However, the presence of a semi-clathrate structure on the surface of ferritin has not been previously reported. Herein, we describe the structural details of a single semiclathrate in a crystal of ferritin that is formed over one specific alanine residue that is exposed to a large solvent channel (Figure 1) in an arrangement similar to the framework observed in Maxi.…”

Section: ■ Introductionmentioning

confidence: 98%

“…Few semi-clathrate structures have been identified experimentally because they exist in narrow spaces or are anchored by interactions with many amino acid residues. ,,, Thus, the mechanisms of the formation of semi-clathrate structures are not yet fully understood. Interactions of ferritin with ice nuclei have been studied by analytical methods such as dynamic light scattering and differential scanning calorimetry. , However, the presence of a semi-clathrate structure on the surface of ferritin has not been previously reported.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Atomic-Level Insights into a Unique Semi-Clathrate Hydrate Formed in a Confined Environment of Porous Protein Crystal

Maity,

Tian,

Furuta

et al. 2023

Crystal Growth & Design

View full text Add to dashboard Cite

Water behavior on protein surfaces influences the protein structure and function. Antifreeze proteins (AFPs) have been intensively studied in the context of biological cytotechnology. AFPs can inhibit the growth of ice microcrystals by forming unique water cluster networks that are influenced by protein surface morphology and hydrophobicity. One such unique water cluster network has been identified as semi-clathrate structures in crystals and is believed to be stabilized by intermolecular interactions within the confined environment. However, there is little atomic-level information about the process of formation of semi-clathrates and the structural units of water-clathrate networks. We identified a single semi-clathrate formed on the pore surface of ferritin crystal, which has a structure similar to that of a natural AFP. Comparison of ferritin mutants and determination of temperature-dependent structures revealed that semi-clathrate water molecules on an α-helix undergo structural alterations with increasing temperatures. Lowering the temperature regenerates the semi-clathrate structure. Water molecules hydrogen-bonded to main chain carbonyl groups are stably immobilized at room temperature and serve as starting points for clathrate formation. These findings provide a mechanistic understanding of water networks in AFPs and guidelines for designing new cryomaterials.

show abstract

Section: Discussionmentioning

confidence: 77%

Section: ■ Discussionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Atomic-Level Insights into a Unique Semi-Clathrate Hydrate Formed in a Confined Environment of Porous Protein Crystal

Maity,

Tian,

Furuta

et al. 2023

Crystal Growth & Design

View full text Add to dashboard Cite

show abstract

“…Interactions of ferritin with ice nuclei have been studied by analytical methods such as dynamic light scattering and differential scanning calorimetry. (25,26) However, the presence of a semi-clathrate structure on the surface of ferritin has not been previously reported.…”

Section: Introductionmentioning

confidence: 96%

Structural insights into a single semi-clathrate hydrate formed in a confined environment of porous protein crystal

Maity

Tian

Furuta

et al. 2023

Preprint

View full text Add to dashboard Cite

Water behavior on protein surfaces influences protein structure and function. Antifreeze Proteins (AFPs) have been intensively studied in context of biological cytotechnology. AFPs inhibit growth of ice microcrystals by forming unique water-cluster networks which are influenced by protein surface morphology and hydrophobicity. Such unique water-cluster networks have been identified as semi-clathrate structures in crystals and are believed to be stabilized by intermolecular interactions within the confined environment. However, there is little atomic-level information about the process of formation of semi-clathrates and the structural units of water-clathrate networks. We identified a single semi-clathrate formed on the pore surface of ferritin crystal which has a structure similar to that of a natural AFP. Comparison of ferritin mutants and determination of temperature-dependent structures revealed that semi-clathrate water molecules on an ⍺-helix undergo structural alterations with increasing temperature. Lowering the temperature regenerates the semi-clathrate structure. Water molecules hydrogen-bonded to main chain carbonyl groups are stably immobilized at room temperature and serve as starting points for clathrate formation. These findings provide a mechanistic understanding of water networks in AFPs and guidelines for designing new cryomaterials.

show abstract

Crystallization of Water on Ferritin – Ice Nucleation by Size, Shape or Surface Chemistry?

Cited by 2 publications

References 0 publications

Atomic-Level Insights into a Unique Semi-Clathrate Hydrate Formed in a Confined Environment of Porous Protein Crystal

Atomic-Level Insights into a Unique Semi-Clathrate Hydrate Formed in a Confined Environment of Porous Protein Crystal

Structural insights into a single semi-clathrate hydrate formed in a confined environment of porous protein crystal

Contact Info

Product

Resources

About