IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Electro-optical properties characterization of Fish Type III Antifreeze Protein
Autor/es:
SALVAY A. G.; SANTOS J.; HOWARD E. I.
Revista:
Journal of Biological Physics
Editorial:
Springer Netherlands
Referencias:
Lugar: Holanda; Año: 2008
ISSN:
0092-0606
Resumen:
Abstract Antifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants and soil bacteria) AFPs play an important role in subzero temperature survival. Fish Type III AFP are present in members of the subclass Zoarcoidei. AFPIII are small 7 kDa –or 14 kDa tandem– globular proteins. In the present work we study the behavior of several physical properties such as low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of inter-particle interactions. Thermal stability and electro-optical behavior when proteins are dissolved in deuterated water were also investigated. point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants and soil bacteria) AFPs play an important role in subzero temperature survival. Fish Type III AFP are present in members of the subclass Zoarcoidei. AFPIII are small 7 kDa –or 14 kDa tandem– globular proteins. In the present work we study the behavior of several physical properties such as low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of inter-particle interactions. Thermal stability and electro-optical behavior when proteins are dissolved in deuterated water were also investigated. point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants and soil bacteria) AFPs play an important role in subzero temperature survival. Fish Type III AFP are present in members of the subclass Zoarcoidei. AFPIII are small 7 kDa –or 14 kDa tandem– globular proteins. In the present work we study the behavior of several physical properties such as low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of inter-particle interactions. Thermal stability and electro-optical behavior when proteins are dissolved in deuterated water were also investigated. Abstract Antifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants and soil bacteria) AFPs play an important role in subzero temperature survival. Fish Type III AFP are present in members of the subclass Zoarcoidei. AFPIII are small 7 kDa –or 14 kDa tandem– globular proteins. In the present work we study the behavior of several physical properties such as low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of inter-particle interactions. Thermal stability and electro-optical behavior when proteins are dissolved in deuterated water were also investigated. Keywords Antifreeze proteins – AFPIII – Electro-optical behavior – Thermal stabilityAntifreeze proteins – AFPIII – Electro-optical behavior – Thermal stability