NMR Research Today is a free monthly online journal that collates and summarizes the latest research about NMR, including details on nuclear magnetic resonance, structural determination, techniques.

Diffusion NMR studies on fish antifreeze proteins and synthetic analogues.

Inglis SR, McGann MJ, Price WS, Harding MM

School of Chemistry, The University of New South Wales, Sydney, NSW 2052, Australia.

Pulsed field gradient spin echo NMR spectroscopy was used to measure diffusion coefficients of the alpha-helical type I antifreeze protein from the winter flounder, two synthetic derivatives in which the four Thr residues were replaced with Val and Ala, respectively, and the low molecular weight fraction antifreeze glycoprotein. Under the conditions studied, the natural type I antifreeze protein and low molecular weight glycoprotein gave diffusion values that were consistent with the presence of monomeric protein in solution. While significant aggregation of the Ala analogue was observed (2-10 mM), there was no evidence for aggregation in the Val analogue (1-3 mM). These results are compared with previously reported solubility and thermal hysteresis data and the implications for the design of synthetic antifreeze proteins are discussed.

Published 3 July 2006 in FEBS Lett, 580(16): 3911-5.
Full-text of this article is available online (may require subscription).

© 2005-2008 NMR Research Today. All Rights Reserved.