Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus

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Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus. / Wilkens, Casper; Poulsen, Jens-Christian Navarro; Ramløv, Hans; Lo Leggio, Leila.

I: Cryobiology, Bind 69, Nr. 1, 2014, s. 163-168.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Wilkens, C, Poulsen, J-CN, Ramløv, H & Lo Leggio, L 2014, 'Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus', Cryobiology, bind 69, nr. 1, s. 163-168. https://doi.org/10.1016/j.cryobiol.2014.07.003

APA

Wilkens, C., Poulsen, J-C. N., Ramløv, H., & Lo Leggio, L. (2014). Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus. Cryobiology, 69(1), 163-168. https://doi.org/10.1016/j.cryobiol.2014.07.003

Vancouver

Wilkens C, Poulsen J-CN, Ramløv H, Lo Leggio L. Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus. Cryobiology. 2014;69(1):163-168. https://doi.org/10.1016/j.cryobiol.2014.07.003

Author

Wilkens, Casper ; Poulsen, Jens-Christian Navarro ; Ramløv, Hans ; Lo Leggio, Leila. / Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus. I: Cryobiology. 2014 ; Bind 69, Nr. 1. s. 163-168.

Bibtex

@article{7df3341e32824ecda9ec6d91cb8c31e8,

title = "Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus",

abstract = "Antifreeze proteins (AFPs) are essential components of many organisms adaptation to cold temperatures. Fish type III AFPs are divided into two groups, SP isoforms being much less active than QAE1 isoforms. Two type III AFPs from Zoarces viviparus, a QAE1 (ZvAFP13) and an SP (ZvAFP6) isoform, are here characterized and their crystal structures determined. We conclude that the higher activity of the QAE1 isoforms cannot be attributed to single residues, but rather a combination of structural effects. Furthermore both ZvAFP6 and ZvAFP13 crystal structures have water molecules around T18 equivalent to the tetrahedral-like waters previously identified in a neutron crystal structure. Interestingly, ZvAFP6 forms dimers in the crystal, with a significant dimer interface. The presence of ZvAFP6 dimers was confirmed in solution by native electrophoresis and gel filtration. To our knowledge this is the first report of dimerization of AFP type III proteins.",

author = "Casper Wilkens and Poulsen, {Jens-Christian Navarro} and Hans Raml{\o}v and {Lo Leggio}, Leila",

year = "2014",

doi = "10.1016/j.cryobiol.2014.07.003",

language = "English",

volume = "69",

pages = "163--168",

journal = "Cryobiology",

issn = "0011-2240",

publisher = "Academic Press",

number = "1",

}

RIS

TY - JOUR

T1 - Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus

AU - Wilkens, Casper

AU - Poulsen, Jens-Christian Navarro

AU - Ramløv, Hans

AU - Lo Leggio, Leila

PY - 2014

Y1 - 2014

N2 - Antifreeze proteins (AFPs) are essential components of many organisms adaptation to cold temperatures. Fish type III AFPs are divided into two groups, SP isoforms being much less active than QAE1 isoforms. Two type III AFPs from Zoarces viviparus, a QAE1 (ZvAFP13) and an SP (ZvAFP6) isoform, are here characterized and their crystal structures determined. We conclude that the higher activity of the QAE1 isoforms cannot be attributed to single residues, but rather a combination of structural effects. Furthermore both ZvAFP6 and ZvAFP13 crystal structures have water molecules around T18 equivalent to the tetrahedral-like waters previously identified in a neutron crystal structure. Interestingly, ZvAFP6 forms dimers in the crystal, with a significant dimer interface. The presence of ZvAFP6 dimers was confirmed in solution by native electrophoresis and gel filtration. To our knowledge this is the first report of dimerization of AFP type III proteins.

AB - Antifreeze proteins (AFPs) are essential components of many organisms adaptation to cold temperatures. Fish type III AFPs are divided into two groups, SP isoforms being much less active than QAE1 isoforms. Two type III AFPs from Zoarces viviparus, a QAE1 (ZvAFP13) and an SP (ZvAFP6) isoform, are here characterized and their crystal structures determined. We conclude that the higher activity of the QAE1 isoforms cannot be attributed to single residues, but rather a combination of structural effects. Furthermore both ZvAFP6 and ZvAFP13 crystal structures have water molecules around T18 equivalent to the tetrahedral-like waters previously identified in a neutron crystal structure. Interestingly, ZvAFP6 forms dimers in the crystal, with a significant dimer interface. The presence of ZvAFP6 dimers was confirmed in solution by native electrophoresis and gel filtration. To our knowledge this is the first report of dimerization of AFP type III proteins.

U2 - 10.1016/j.cryobiol.2014.07.003

DO - 10.1016/j.cryobiol.2014.07.003

M3 - Journal article

C2 - 25025819

VL - 69

SP - 163

EP - 168

JO - Cryobiology

JF - Cryobiology

SN - 0011-2240

IS - 1

ER -

ID: 128608120

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