Effects of bound antifreeze proteins on equilibrium configuration of ice-liquid interface

Author

Liu, Junjie ; Xie, Wenjing

Author_Institution

Sch. of Phys. Sci. & Technol., Inner Mongolia Univ., Hohhot, China

Volume

6

fYear

2010

fDate

16-18 Oct. 2010

Firstpage

2556

Lastpage

2559

Abstract

Experimentations reveal that antifreeze proteins (AFPs) in solution can bind on ice surface and shape the ice crystals. Based on the theory of ice crystal growth, the shape of an ice crystal is determined by its most slowly growing faces. If the driven force of phase transformation is given, the growth rate of each face is determined by the configuration of ice-liquid interface. The effects of bound AFPs on equilibrium configuration of ice-liquid interface have been obtained by using the theory of polymer chemistry. The results suggest that sharp rough ice-liquid interfaces of binding AFPs translate into sharp singular interfaces.

Keywords

coolants; crystal binding; crystal growth; crystallisation; ice; proteins; bound antifreeze proteins; equilibrium configuration; ice crystal growth; ice surface binding; ice-liquid interface; phase transformation; polymer chemistry; solutions; Anti-freeze; Crystals; Hysteresis; Ice; Nickel; Proteins; Shape; antifreeze proteins; configuration; ice-liquid interface;

fLanguage

English

Publisher

ieee

Conference_Titel

Biomedical Engineering and Informatics (BMEI), 2010 3rd International Conference on

Conference_Location

Yantai

Print_ISBN

978-1-4244-6495-1

Type

conf

DOI

10.1109/BMEI.2010.5639717

Filename

5639717