Structure-Function Studies of Native and Recombinant Fish Antifreeze Proteins.
Abstract
This project investigates the structures of several fish antifreeze proteins, and how they interact with ice crystals and inhibit ice growth. Formation of hexagonal pit formation on ice crystal basal plane in the presence of fish antifreeze proteins was examined with two-photon fluorescence imaging which showed binding of antifreeze glycoproteins molecules on pit faces; the origin of pit development presumably stems from antifreeze adsorption on dislocations on the basal plane. A novel ice-active protein was isolated from AFGP-bearing notothenioid fish and its partial structure was determined. This protein and AFGP together lead to synergistic augmentation of antifreeze activity and thus has potential bearing on the design of more potent anti-freezing systems. A putative new type of antifreeze peptide was isolated from an Arctic liparid fish and its partial sequence was determined. And lastly, the X-ray crystallographic structure of a type III antifreeze peptide from an Antarctic eel pout and the protein's ice-binding surface were determined.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 16, 2000
- Accession Number
- ADA376060
Entities
People
- Arthur L. Devries
- Chi-hing C. Cheng-devries
Organizations
- University of Illinois Urbana–Champaign