Dynamics of oligomer formation by denatured carbonic anhydrase II

Prokhorov, Dmitry; Timchenko, A. A.; Uversky, Vladimir N.; Khristoforov, V. S.; Kihara, Hiroshi; Kimura, Kazumoto; Kutyshenko, V. P.

doi:10.1016/j.bbapap.2008.02.012

Cited by 7 publications

(5 citation statements)

References 73 publications

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“…Such oligomers are ultimately assembled into a gel-like structure. 55 Formation of similar (amyloid) fibrils, sheaths and hydrogel-like structures has been observed during in vitro biomineralization of CaCO 3 in the presence of nacre 43 and sea urchin spicule matrix proteins. 13,44 Such supramolecular protein structures, whose self-assembly appears to be induced/facilitated by Ca 2+ ions, have been shown to direct CaCO 3 precipitation via dense liquid and amorphous solid precursor phases, 13 and induce the oriented heterogeneous nucleation of crystalline calcium carbonate phases, especially in the case of Asp-and Glu-rich matrix proteins.…”

Section: Discussionmentioning

confidence: 99%

The multiple roles of carbonic anhydrase in calcium carbonate mineralization

Rodríguez-Navarro

Çizer

Kudłacz³

et al. 2019

CrystEngComm

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Section: Discussionmentioning

confidence: 99%

The multiple roles of carbonic anhydrase in calcium carbonate mineralization

Rodríguez-Navarro

Çizer

Kudłacz³

et al. 2019

CrystEngComm

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“…CAB is a small (MW ≈ 29 kDa) zinc metalloenzyme that catalyzes the hydration of carbon dioxide and hydrolysis of esters. , It has been shown to refold slowly in water (half time of several minutes up to ca. 10 h, with a molten globule intermediate state) and to undergo intermolecular association and irreversible aggregation when it is unfolded. , Assemblies with amphiphiles (surfactants) enhance dramatically the solubility of CAB during its renaturation from urea solutions, and can yield high (>80%) regains of activity, suggesting that control of hydrophobic associations contributes to correct refolding. Ionic surfactants are however significantly more efficient than nonionic ones, suggesting a contribution of Coulombic repulsion.…”

Section: Introductionmentioning

confidence: 99%

Prevention of Aggregation and Renaturation of Carbonic Anhydrase via Weak Association with Octadecyl- or Azobenzene-Modified Poly(acrylate) Derivatives

2014

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The prevention of aggregation during renaturation of urea-denatured carbonic anhydrase B (CAB) via hydrophobic and Coulomb association with anionic polymers was studied in mixed solutions of CAB and amphiphilic poly(acrylate) copolymers. The polymers were derivatives of a parent poly(acrylic acid) randomly grafted with hydrophobic side groups (either 3 mol % octadecyl group, or 1-5 mol % alkylamidoazobenzene photoresponsive groups). CAB:polymer complexes were characterized by light scattering and fluorescence correlation spectroscopy in aqueous buffers (pH 7.75 or 5.9). Circular dichroism and enzyme activity assays enabled us to study the kinetics of renaturation. All copolymers, including the hydrophilic PAA parent chain, provided a remarkable protective effect against CAB aggregation during renaturation, and most of them (but not the octadecyl-modified one) markedly enhanced the regain of activity as compared to CAB alone. The significant role of Coulomb binding in renaturation and comparatively the lack of efficacy of hydrophobic association was highlighted by measurements of activity regain before and after in situ dissociation of hydrophobic complexes (achieved by phototriggering the polarity of azobenzene-modified polymers under exposure to UV light). In the presence of polymers (CAB:polymer of 1:1 w/w ratio) at concentration ∼0.6 g L(-1), the radii of the largest complexes were similar to the radii of the copolymers alone, suggesting that the binding of CAB involves one or a few polymer chain(s). These complexes dissociated by dilution (0.01 g L(-1)). It is concluded that prevention of irreversible aggregation and activity recovery were achieved when marginally stable complexes are formed. Reaching a balanced stability of the complex plays the main role in CAB renaturation, irrespective of the nature of the binding (by Coulomb association, with or without contribution of hydrophobic association).

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“…This observation can be explained by the increased concentration of such amino acids in comparison with the original extract and also by the fact that the lines corresponding to such amino acids are noticeably broader than lines corresponding to the free amino acids in the extract. Furthermore, the characteristic feature of globular proteins is the presence of very pronounced signals in the pool of methyl protons, which are much more intensive than the rest of the spectrum, a behavior especially characteristic of the denatured proteins [10].…”

Section: Resultsmentioning

confidence: 99%

“In-plant” NMR: Analysis of the Intact Plant Vesicularia dubyana by High Resolution NMR Spectroscopy

2015

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Abstract:We present here the concept of "in-plant" NMR and show that high-resolution NMR spectroscopy is suitable for the analysis of intact plants and can be used to follow the changes in the intraorganismal molecular composition over long time periods. The NMR-based analysis of the effect of different concentrations of heavy water on the aquatic plant Vesicularia dubyana revealed that due to the presence of specific adaptive mechanisms this plant can sustain the presence of up to 85% of D2O. However, it dies in 100% heavy water.

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Dynamics of oligomer formation by denatured carbonic anhydrase II

Cited by 7 publications

References 73 publications

The multiple roles of carbonic anhydrase in calcium carbonate mineralization

The multiple roles of carbonic anhydrase in calcium carbonate mineralization

Prevention of Aggregation and Renaturation of Carbonic Anhydrase via Weak Association with Octadecyl- or Azobenzene-Modified Poly(acrylate) Derivatives

“In-plant” NMR: Analysis of the Intact Plant Vesicularia dubyana by High Resolution NMR Spectroscopy

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