1. The type I antifreeze protein bpAFP from barfin plaice has two forms of ice binding at different concentrations. It binds to the pyramidal planes at low concentrations and to the whole ice crystal surface including the basal planes at high concentrations.
2. bpAFP shows moderately active at low concentrations and transforms into hyperactive at high concentrations. Its thermal hysteresis activity increases significantly with the increase of concentration.
AFP011002
General Information
| Protein Name | Liposetta pinnifasciata AFP |
| UniProt ID | UPI000C212033 |
| Species | Liposetta pinnifasciata |
| Sequence Length | 40 |
| Sequence | |
| Structure | AF2 predicted Structure: AFP011002 |
| Solvent Accessible Surface Area | Total SASA | 2312.24 Ų | Polar SASA | 814.04 Ų | Apolar SASA | 3126.27 Ų |
AFP011002000
| Mutation | Wild Type |
| Sequence |
Ice crystal morphology
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | native bpAFP |
| Ice crystal morphology | Fig.1.D Hexagonal trapezohedral ice crystal formed in 0.25 mg·mL⁻¹ of the bpAFP solution; |
Ice crystal morphology
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | rbpAFP |
| Ice crystal morphology | Fig.2.C-D (C)Bursting ice crystal growth along the c-axis observed at the TH limit of 5 mg/mL of rbpAFP; (D)Bursting ice crystal growth perpendicular to c-axis observed for 150 mg/mL of rbpAFP with illustrated interpretations; |
Ice crystal morphology
| PMID | 30048129 |
| DOI | 10.1021/acs.jpclett.8b01492 |
| Protein Name | barfin plaice AFP-I |
| Ice crystal morphology | "For comparison, we also took powder X-ray diffraction patterns of pure hexagonal ice. " |
Thermal Hysteresis
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | native bpAFP |
| Thermal Hysteresis | Fig.2.A-B Ice binding ability and burst pattern of bpAFP: TH plot as a function of the concentration of native bpAFP (open circles) and rbpAFP (black dots) in the range of (a) 0-200 mg/mL and (b) 0-20 mg/mL. The TH values of ordinary type I AFP (wfAFP)35 is plotted in panel (b) for comparison (open squares). (c) Bursting ice crystal growth along the c-axis observed at the TH limit of 5 mg/mL of rbpAFP. (d) Bursting ice crystal growth perpendicular to c-axis observed for 150 mg/mL of rbpAFP with illustrated interpretations. |
Thermal Hysteresis
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | rbpAFP |
| Thermal Hysteresis | Fig.2.A-B Ice binding ability and burst pattern of bpAFP: TH plot as a function of the concentration of native bpAFP (open circles) and rbpAFP (black dots) in the range of (a) 0-200 mg/mL and (b) 0-20 mg/mL. The TH values of ordinary type I AFP (wfAFP)35 is plotted in panel (b) for comparison (open squares). (c) Bursting ice crystal growth along the c-axis observed at the TH limit of 5 mg/mL of rbpAFP. (d) Bursting ice crystal growth perpendicular to c-axis observed for 150 mg/mL of rbpAFP with illustrated interpretations. |
Thermal Hysteresis
| PMID | 32182859 |
| DOI | 10.3390/biom10030423 |
| Protein Name | barfin plaice AFP I |
| Thermal Hysteresis | Fig.2.C-D (C) Weight-base concentration dependence of thermal hysteresis (℃) of AFPI-III and AFGP.It was obtained for up to 50 mg/mL for AFPIII and 200 mg/mL for the others, as one single crystal was difficult to prepare above these concentrations. (D)Molar-base concentration dependence of thermal hysteresis (℃) of AFPI-III and AFGP. For these plots, 3300;14,000; 6500; and 12,000 Da were assumed as the average molecular weights for the native AFPI-III and AFGP samples, respectively. |
Fluorescence-based Ice Plane Affinity
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | native bpAFP |
| Fluorescence-based Ice Plane Affinity | Fig.3.A-B Ice plane affinity of bpAFP:(a)Fluorescence-based ice plane affinity (FIPA) analysis of rhodamine®tagged-bpAFP at a concentration of 0.02 mg·mL⁻¹ (i) and its interpreted illustration (ii). The direction of the c-axis out of the plane of the figure is indicated by the white dot in the circle.(b)Change of the FIPA pattern with increasing bpAFP concentration. Upper (i-v) and lower panels (v-iii) show top and side views of an ice hemisphere, respectively, as guided by c-axis direction. |
Fluorescence-based Ice Plane Affinity
| PMID | 32182859 |
| DOI | 10.3390/biom10030423 |
| Protein Name | barfin plaice AFP I |
| Fluorescence-based Ice Plane Affinity | Fig.3.A Illustration of the known FIPA pattern of AFP I. Inclined ellipses implying the AFP I binding to ice pyramidal planes were overcast by an entire illumination that progressed on the spherical ice afterincreasing the concentration from 0.01 to 0.1 mg/mL. |
Ice plane
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | native bpAFP |
| Ice plane | The Ice-plane contains the whole ice crystal surface, including the basal planes. |
Ice plane
| PMID | 28211917 |
| DOI | 10.1038/srep42501 |
| Protein Name | rbpAFP |
| Ice plane | The Ice-plane contains the whole ice crystal surface, including the basal planes. |
Ice plane
| PMID | 32182859 |
| DOI | 10.3390/biom10030423 |
| Protein Name | barfin plaice AFP I |
| Ice plane | The Ice-plane contains ice pyramidal planes. |
Ice plane
| PMID | 30048129 |
| DOI | 10.1021/acs.jpclett.8b01492 |
| Protein Name | barfin plaice AFP-I |
| Ice plane | It binds to the (2 0 2_ 1) pyramidal plane of a single hexagonal ice crystal. |
Brief description
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PMID: 28211917
DOI: 10.1038/srep42501 |
|
|
PMID: 32182859
DOI: 10.3390/biom10030423 |
1. At low concentrations, AFP I binds to the pyramidal plane of ice. At high concentrations, it can bind to multiple ice planes.
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PMID: 30048129
DOI: 10.1021/acs.jpclett.8b01492 |
1. The ice crystallites formed from AFP-I solutions have a bipyramidal shape.
2. AFP-I increases the glass transition temperature (Tg) by approximately 30 K, likely by influencing proton migration and stabilizing ice structure, revealing its potential role in cold adaptation. |