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