The quasi-liquid layer involvement in antifreeze function

COMP 13

Yin Yeh, yyeh@ucdavis.edu, Department of Applied Science, Univeristy of California-Davis, One Shields Avenue, Davis, CA 95616, Krish Krishnan, krish@csufresno.edu, Department of Chemistry, California State University Fresno/Univerisity of California Davis, SB-70 East San Ramon Road, Fresno, CA 93740, William H. Fink, Chemistry, University of California, and Yong Duan, duan@ucdavis.edu, Genome Center and Department of Applied Science, University of California, Davis, One Shields Avenue, Davis, CA 95616.
Feeney et al. had suggested in 1972 that researchers should maintain an open mind on the possibility that the then only known antifreeze protein, the AFGP, might function with its hydrophobic methyl facet closer toward the ice than the disaccharide groups. Experimental evidence is now mounting to suggest that the mechanism of action in both freezing point depression and ice growth facet modification requires a close coupling between entropic and enthalpic contributions. We propose that a strong entropic contribution resides in the existence of the ubiquitous quasi-liquid layer (QLL), which has been strongly suggested in studies of the pure ice-water system as well as surface-sensitive studies involving antifreeze proteins. QLL allows for proteins that are intrinsically disordered to reside in a favorable entropic environment while contributing to function, consistent with the idea that the many conformational states may play important roles in energy exchange when surface binding affinity is low.
 

Antifreeze Proteins: A Memorial Symposium for Robert Feeney
8:30 AM-12:05 PM, Sunday, August 19, 2007 BCEC -- 162A, Oral

Division of Computers in Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007