Antifreeze Glycoproteins to function as intrinsically unstructured proteins

COMP 18

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, Yin Yeh, yyeh@ucdavis.edu, Department of Applied Science, Univeristy of California-Davis, One Shields Avenue, Davis, CA 95616, Yong Duan, duan@ucdavis.edu, Applied Science, University of California Davis, Davis, CA 95616, and William H. Fink, Chemistry, University of California.
The flexibility of a protein is closely coupled to its function. The structure of intrinsically unstructured proteins (IUP) resembles the denatured states of ordered proteins, best described as an ensemble of rapidly inter-converting alternative structures, which, nevertheless, is their native, functional state. It is becoming increasingly clear that biological activity is not restricted to compact semi-rigid proteins. Often, their function is realized via molecular recognition in which structural disorder confers specific advantages, such as increased speed of interaction and specificity without excessive binding strength. However, there is considerable challenge in their nature and how best to characterize them to understand their functional significance. Our recent NMR based diffusion coefficient measurements in supercooled water, relaxation rate measurements in both supercooled water and in the presence of ice and computer simulations showed that AFGP-8 retains flexible conformations, consistent with the idea they may function as IUPs.
 

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