Experimental correlation between thermal hysteresis activity and the distance between antifreeze proteins on an ice surface

RSC Advances ◽  
2015 ◽  
Vol 5 (11) ◽  
pp. 7848-7853 ◽  
Author(s):  
Ran Drori ◽  
Peter L. Davies ◽  
Ido Braslavsky
Keyword(s):  
Fluorescence Microscopy ◽  
Thermal Hysteresis ◽  
Freezing Point ◽  
Antifreeze Proteins ◽  
Microfluidic Devices ◽  
Freezing Point Depression ◽  
Thermal Hysteresis Activity ◽  
Ice Surface ◽  
Experimental Correlation ◽  
Temperature Controlled

Temperature-controlled microfluidic devices and fluorescence microscopy illustrate the correlation between freezing-point depression and the distance between antifreeze proteins on an ice surface.

scholarly journals Ice Growth Acceleration by Antifreeze Proteins Leads to Higher Thermal Hysteresis Activity

2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori
Keyword(s):  
Crystal Growth ◽  
Growth Inhibition ◽  
Growth Velocity ◽  
Crystal Morphology ◽  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Ice Crystal ◽  
Ice Growth ◽  
Thermal Hysteresis Activity ◽  
Adsorption Rates

<p>Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the <i>c</i>-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the <i>c</i>-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a></p>

Seasonal changes in the plasma levels of glycoprotein antifreeze, Na+, Cl−, and glucose in Newfoundland Atlantic cod (Gadus morhua)

1982 ◽  
Vol 60 (8) ◽  
pp. 1851-1854 ◽  
Author(s):  
G. L. Fletcher ◽  
D. Slaughter ◽  
C. L. Hew
Keyword(s):  
Seasonal Changes ◽  
Gadus Morhua ◽  
Thermal Hysteresis ◽  
Atlantic Cod ◽  
Freezing Point ◽  
Freezing Point Depression ◽  
Antifreeze Glycoproteins ◽  
Glucose Levels ◽  
Total Plasma Protein ◽  
Two Peaks

A seasonal study was carried out on the hematocrits, plasma freezing point depression, and thermal hysteresis, and plasma Na+, Cl−, total protein, and glucose concentrations in laboratory maintained Atlantic cod. Significant thermal hysteresis was evident in the plasma during the months of January to May indicating the presence of antifreeze glycoproteins. Plasma freezing point depression and Na+ and Cl− concentrations were highest during the winter months and lowest during the summer. Two peaks in glucose levels were evident; one in February and the other in July. No seasonal changes were evident in hematocrits and total plasma protein concentrations.

Discovery of an antifreeze protein in the leaves of Ammopiptanthus nanus

2010 ◽  
Vol 90 (1) ◽  
pp. 35-40 ◽  
Author(s):  
S. Yu ◽  
L. Yin ◽  
S. Mu
Keyword(s):  
Differential Scanning Calorimetry ◽  
Thermal Hysteresis ◽  
Large Subunit ◽  
Antifreeze Proteins ◽  
Cold Climate ◽  
High Definition ◽  
Scanning Calorimetry ◽  
Bisphosphate Carboxylase ◽  
Thermal Hysteresis Activity ◽  
Ammopiptanthus Nanus

Overwintering plants produce antifreeze proteins (AFPs) that allow plants to survive under freezing or sub-freezing conditions. Ammopiptanthus nanus (M. Pop.) Cheng f. grows in the desert of Xinjiang, P.R. China, and our objective was to determine if its survival was dependent on AFP and to identify the protein. Using anion exchange and gel filtration, the AFP was extracted, isolated and purified from cold-acclimated A. nanus leaves. The thermal hysteresis activity (THA) of the antifreeze proteins was measured by differential scanning calorimetry. The THA of the AFP was 0.46°C when the concentration of the protein was 20 mg mL-1. The molecular weight of a band was about 119.24 kDa in SDS-PAGE gel. We detected (P < 0.05) the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit by analyzing the 119.24 kDa protein using the Waters SYNAPT™ high definition mass spectrometry (HDMS™) System. Our results indicate that there is an AFP in A. nanus leaves, and that it may play a vital role as a defence against the cold climate, thus increasing the chances for survival of A. nanus in its desert habitat.Key words: Thermal hysteresis activity, differential scanning calorimetry, extraction, purification, cold climate, desert habitat

scholarly journals Ice Growth Acceleration by Antifreeze Proteins Leads to Higher Thermal Hysteresis Activity

2020 ◽  
Vol 124 (49) ◽  
pp. 11081-11088
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori
Keyword(s):  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Ice Growth ◽  
Thermal Hysteresis Activity

scholarly journals A two-dimensional adsorption kinetic model for thermal hysteresis activity in antifreeze proteins

2006 ◽  
Vol 124 (20) ◽  
pp. 204702 ◽  
Author(s):  
Q. Z. Li ◽  
Y. Yeh ◽  
J. J. Liu ◽  
R. E. Feeney ◽  
V. V. Krishnan
Keyword(s):  
Kinetic Model ◽  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Adsorption Kinetic ◽  
Two Dimensional ◽  
Thermal Hysteresis Activity ◽  
Adsorption Kinetic Model

scholarly journals Ice Growth Acceleration by Antifreeze Proteins Leads to Higher Thermal Hysteresis Activity

2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori
Keyword(s):  
Crystal Growth ◽  
Growth Inhibition ◽  
Growth Velocity ◽  
Crystal Morphology ◽  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Ice Crystal ◽  
Ice Growth ◽  
Thermal Hysteresis Activity ◽  
Adsorption Rates

<p>Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the <i>c</i>-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the <i>c</i>-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a></p>

scholarly journals Enhancement of insect antifreeze protein activity by solutes of low molecular mass.

1998 ◽  
Vol 201 (15) ◽  
pp. 2243-2251 ◽  
Author(s):  
N Li ◽  
C A Andorfer ◽  
J G Duman
Keyword(s):  
Molecular Mass ◽  
Thermal Hysteresis ◽  
Specific Activity ◽  
Freezing Point ◽  
Consensus Sequence ◽  
Ammonium Bicarbonate ◽  
Amino Acid Residues ◽  
Protein Activity ◽  
Dendroides Canadensis ◽  
Thermal Hysteresis Activity

Antifreeze proteins (AFPs) lower the non-equilibrium freezing point of water (in the presence of ice) below the melting point, thereby producing a difference between the freezing and melting points that has been termed thermal hysteresis. In general, the magnitude of the thermal hysteresis depends upon the specific activity and concentration of the AFP. This study describes several low-molecular-mass solutes that enhance the thermal hysteresis activity of an AFP from overwintering larvae of the beetle Dendroides canadensis. The most active of these is citrate, which increases the thermal hysteresis nearly sixfold from 1.2 degrees C in its absence to 6.8 degrees C. Solutes which increase activity approximately fourfold are succinate, malate, aspartate, glutamate and ammonium sulfate. Glycerol, sorbitol, alanine and ammonium bicarbonate increased thermal hysteresis approximately threefold. Interestingly, 0.5 mol l-1 sodium sulfate eliminated activity. Solute concentrations between 0.25 and 1 mol l-1 were generally required to elicit optimal thermal hysteresis activity. Glycerol is the only one of these enhancing solutes that is known to be present at these concentrations in overwintering D. canadensis, and therefore the physiological significance of most of these enhancers is unknown. The mechanism(s) of this enhancement is also unknown. The AFP used in this study (DAFP-4) is nearly identical to previously described D. canadensis AFPs. The mature protein consists of 71 amino acid residues arranged in six 12- or 13-mer repeats with a consensus sequence consisting of Cys-Thr-X3-Ser-X5-X6-Cys-X8-X9-Ala-X11-Thr-X1 3, where X3 and X11 tend to be charged residues, X5 tends to be Thr or Ser, X6 to be Asn or Asp, X9 to be Asn or Lys and X13 to be Ala in the 13-mers. DAFP-4 is shorter by one repeat than previously described D. canadensis AFPs.

NMR structural studies on antifreeze proteins

1998 ◽  
Vol 76 (2-3) ◽  
pp. 284-293 ◽  
Author(s):  
Frank D Sönnichsen ◽  
Peter L Davies ◽  
Brian D Sykes
Keyword(s):  
Freezing Point ◽  
Antifreeze Proteins ◽  
Isotopic Labeling ◽  
Inhibition Mechanism ◽  
Structural Studies ◽  
Nmr Analysis ◽  
Ice Surface ◽  
Nmr Data ◽  
Ice Binding ◽  
Nmr Techniques

Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of ~1°C, which is sufficient to prevent fish from freezing in ice-laden seawater, requires millimolar AFP levels in the blood. The solubility of AFPs at these millimolar concentrations and the small size of the AFPs (typically 3-15 kDa) make them ideal subjects for NMR analysis. Although fish AFPs are naturally abundant, seasonal expression, restricted access to polar fishes, and difficulties in separating numerous similar isoforms have made protein expression the method of choice for producing AFPs for structural studies. Expression of recombinant AFPs has also facilitated NMR analysis by permitting isotopic labeling with 15N and 13C and has permitted mutations to be made to help with the interpretation of NMR data. NMR analysis has recently solved two AFP structures and provided valuable information about the disposition of ice-binding side chains in a third. The potential exists to solve other AFP structures, including the newly described insect AFPs, and to use solid-state NMR techniques to address fundamental questions about the nature of the interaction between AFPs and ice.Key words: NMR spectroscopy, antifreeze, ice-binding affinity, review.

scholarly journals DSC Study on the Thermal Hysteresis Activity of Plant Antifreeze Proteins

2001 ◽  
Vol 17 (01) ◽  
pp. 66-69
Author(s):  
Zhou Xiao-Lei ◽  
◽  
Chen Tao-Tao ◽  
Wang Bao-Huai ◽  
Li Zhi-Fen ◽  
...  
Keyword(s):  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Thermal Hysteresis Activity ◽  
Plant Antifreeze Proteins

Thermal hysteresis activity of antifreeze proteins: A model based on fractional statistics theory of adsorption

2021 ◽  
Vol 575 ◽  
pp. 126046
Author(s):  
J.I. Lopez Ortiz ◽  
E. Quiroga ◽  
C.F. Narambuena ◽  
J.L. Riccardo ◽  
A.J. Ramirez-Pastor
Keyword(s):  
Thermal Hysteresis ◽  
Antifreeze Proteins ◽  
Fractional Statistics ◽  
Model Based ◽  
Thermal Hysteresis Activity
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