Purification and structural analysis of a type III antifreeze protein from the european eelpout Zoarces viviparus.
Cryo Letters
; 28(1): 51-60, 2007.
Article
en En
| MEDLINE
| ID: mdl-17369962
ABSTRACT
It has recently been reported that the eelpout Zoarces viviparus synthesizes a family of antifreeze proteins (AFP) similar in sequence to type III AFPs. A method has been set up to separate these antifreeze proteins from blood serum of this teleost species. A total of nine proteins with antifreeze activity have been isolated, several to a purity suited for NMR experiments. One of the proteins, Zvafp13, has been subject to partial structure determination by NMR. 1D- and 2D-H NMR analyses were carried out. In the 1D-experiments it was observed that the protein contained 28 slow-exchanging amides, suggesting a compact structure. The 2D-experiments were utilized to assign observed signals to specific amino acids. From TOCSY- and NOESY-experiments 35 out of a total of 66 amino acids were assigned. The amide exchange pattern, protein primary sequence, chemical shifts and NOE-cross-peaks between amides and -protons in the -sheets suggest that Zvafp13 structurally resembles the recombinant type III AFP rQAE m1.1.
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Base de datos:
MEDLINE
Asunto principal:
Perciformes
/
Proteínas Anticongelantes Tipo III
Idioma:
En
Revista:
Cryo Letters
Asunto de la revista:
BIOLOGIA
/
QUIMICA
Año:
2007
Tipo del documento:
Article