The mechanism by which fish antifreeze proteins cause thermal hysteresis

Kristiansen, Erlend; Zachariassen, Karl Erik

doi:10.1016/j.cryobiol.2005.07.007

Cited by 185 publications

(171 citation statements)

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“…17 These authors suggested a twostep mechanism for AFP interaction with ice. According to their hypothesis, the first step, which takes place at the equilibrium melting temperature, is equilibrium distribution of AFP molecules between the bulk solution and the interfacial region of ice and water.…”

Section: Discussionmentioning

confidence: 99%

“…At temperatures in the TH gap, the curved ice surface is at equilibrium with the surrounding water, and it is stabilized by perseveringly adhered AFP molecules that are assumed to be "locked" onto the ice surface. 17 This surface can adsorb additional AFP molecules reversibly. In the rare events of engulfment or detachment of a locked molecule, local growth occurs, which can be arrested by another adsorbed AFP molecule that in turn becomes locked onto the surface.…”

Section: Discussionmentioning

confidence: 99%

“…The hydrophobicity of AFP ice-binding faces favors incorporation of AFP molecules into the interfacial region between ice and water, and higher hydrophobicity is associated with decreased solubility and increased affinity to ice. 17 If hydrophobic interactions of the γ-methyl groups with ice were a sufficient driving force for adsorption, we would expect this mutant to retain some TH activity or at least to induce ice faceting during growth or melting. The complete impotence of V a-h suggests that hydrophobic interactions are insufficient for ice binding by TmAFP.…”

Section: Discussionmentioning

confidence: 99%

“…15 Some of these issues have been attended to in kinetic models based either on reversible 16 or irreversible 12 adsorption of AFP molecules to ice, or even a combination of the two. 17 A large number of biochemical, biophysical, and structural studies have been conducted to elucidate the mechanism by which AFPs bind to specific planes of ice. It is established that shape complementarity between AFPs and the ice lattice is crucial for ice binding by both moderately active and hyperactive AFPs.…”

Section: Introductionmentioning

confidence: 99%

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Interactions of β-Helical Antifreeze Protein Mutants with Ice

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Celik

Fass

et al. 2008

Crystal Growth & Design

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ABSTRACT:The fold of the -helical antifreeze protein from Tenebrio molitor (TmAFP) proved to be surprisingly tolerant of multiple amino acid substitutions, enabling the construction of a panel of mutants displaying grids of single amino acid types in place of the threonines on the ice-binding face. These mutants, maintaining the regularity of amino acid spacing found in the wildtype protein but with different functional groups on the surface, were tested for antifreeze activity by measuring thermal hysteresis and observing ice grown in their presence. We found that no mutant exhibited the dramatic activity of the wild-type version of this hyperactive antifreeze protein. However, mutants containing four valines or tyrosines in place of the threonines in the center of the TmAFP ice-binding face showed residual thermal hysteresis activity and had marked effects on ice crystal morphology. The results are discussed in the context of a two-stage model for the absorption-inhibition mechanism of antifreeze protein binding to ice surfaces.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Interactions of β-Helical Antifreeze Protein Mutants with Ice

Bar

Celik

Fass

et al. 2008

Crystal Growth & Design

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“…The mechanism by which 11 antifreeze proteins contribute to thermal hysteresis in fish is not completely understood. Some explanations of this phenomenon suggest the reduction of the solubility of the antifreeze proteins in the solution as one of the causes of hysteretic activity [63]. Other studies [26,64] identify N14, T18 and Q44 as the key residues for antifreeze protein (type III) -ice interaction and reveal the amphipathic character of the ice-binding site.…”

Section: Antifreeze Proteinsmentioning

confidence: 99%

“Fuzzy oil drop” model applied to individual small proteins built of 70 amino acids

2010

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To cite this version:Katarzyna Prymula, Kinga Salapa, Irena Roterman. "Fuzzy oil drop" model applied to individual small proteins built of 70 amino acids. Journal of Molecular Modeling, Springer Verlag (Germany), 2010, 16 (7) Abstract: The proteins composed of short polypeptides (about 70 amino acid residues) representing the following functional groups (according to PDB notation): growth hormones, serine protease inhibitors, antifreeze proteins, chaperones and proteins of unknown function, were selected for structural and functional analysis. Classification based on the distribution of hydrophobicity in terms of deficiency/excess as the measure of structural and functional specificity is presented. The experimentally observed distribution of hydrophobicity in the protein body is compared to the idealized one expressed by a three-dimensional Gauss function. The differences between these two distributions reveal the specificity of structural/functional characteristics of the protein. The residues of hydrophobicity deficiency versus the idealized distribution are assumed to indicate cavities with the potential to bind ligands, while the residues of hydrophobicity excess are interpreted as potentially participating in protein-protein complexation. The distribution of hydrophobicity irregularity seems to be specific for particular structures and functions of proteins. A comparative analysis of such profiles is carried out to identify the potential biological activity of proteins of unknown function.Response to Reviewers: Comments to the reviewers Reviewer #1The sentence "protein structure determines its biological function" got changed to the form : "The spatial distribution of amino acid residues and particularly distribution of their specific hydrophobicity in a protein structure is assumed to influence the biological function". Reviewer #2Ad.1. The section INTRODUCTION has been modified making the problem of NBP less exposed. The paper describing the structures of NBP form is in press currently. The appearance of that paper will make clear the idea of NBP and the usefulness of the presented method. The real proteins available in PDB allowed the comparative analysis of the NBP proteins reveling some substantial differences and similarities between these two groups of proteins position #18 on the reference list (Prymula K, Piwowar M, Kochanczyk M, Flis L, Malawski M, Szepieniec T, Evangelista G, Minervini G, Polticelli F, Wisniowski Z, Salapa K, Matczynska E, and Roterman I (2009) In silico structural study of random amino acid sequence proteins not present in nature. Chem Biodivers, in press). Ad.2. The hydrophobicity scaleThe hydrophobicity scales (theoretical and experimental) were compared in details in respect to "fuzzy oil drop" model in other publication. The "fuzzy oil drop" estimates the hydrophobicity distribution in the very simplified and averaged form. In result, the relative distribution of hydrophobicity is under consideration. The differences observed between different scales get marginal in this st...

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Hibernation: Poikilotherms

Storey

2011

Encyclopedia of Life Sciences

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BackgroundThe standard treatment for patients with diffuse large-B-cell lymphoma is cyclophosphamide, doxorubicin, vincristine, and prednisone (CHOP). Rituximab, a chimeric monoclonal antibody against the CD20 B-cell antigen, has therapeutic activity in diffuse large-B-cell lymphoma. We conducted a randomized trial to compare CHOP chemotherapy plus rituximab with CHOP alone in elderly patients with diffuse large-B-cell lymphoma. Methods Previously untreated patients with diffuselarge-B-cell lymphoma, 60 to 80 years old, were randomly assigned to receive either eight cycles of CHOP every three weeks (197 patients) or eight cycles of CHOP plus rituximab given on day 1 of each cycle (202 patients). ResultsThe rate of complete response was significantly higher in the group that received CHOP plus rituximab than in the group that received CHOP alone (76 percent vs. 63 percent, P=0.005). With a median follow-up of two years, event-free and overall survival times were significantly higher in the CHOP-plusrituximab group (P<0.001 and P=0.007, respectively). The addition of rituximab to standard CHOP chemotherapy significantly reduced the risk of treatment failure and death (risk ratios, 0.58 [95 percent confidence interval, 0.44 to 0.77] and 0.64 [0.45 to 0.89], respectively). Clinically relevant toxicity was not significantly greater with CHOP plus rituximab. ConclusionsThe addition of rituximab to the CHOP regimen increases the complete-response rate and prolongs event-free and overall survival in elderly patients with diffuse large-B-cell lymphoma, without a clinically significant increase in toxicity. (N Engl J Med 2002;346:235-42.)

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The mechanism by which fish antifreeze proteins cause thermal hysteresis

Cited by 185 publications

References 68 publications

Interactions of β-Helical Antifreeze Protein Mutants with Ice

Interactions of β-Helical Antifreeze Protein Mutants with Ice

“Fuzzy oil drop” model applied to individual small proteins built of 70 amino acids

Hibernation: Poikilotherms

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