TAILIEUCHUNG - Báo cáo Y học: Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein

The solution structure of a synthetic mutant type I antifreeze protein (AFP I) was determined in aqueous solution at pH using nuclear magnetic resonance (NMR) spectroscopy. The mutations comprised the replacement of the four Thr residues by Val and the introduction of two additional Lys-Glu salt bridges. The antifreeze activity of this mutant peptide, VVVV2KE, has been previously shown to be similar to that of the wild type protein, HPLC6 (defined here as TTTT). The solution structure reveals an a helix bent in the same direction as the more bent conformer of the published crystal structure of TTTT, while. | Eur. J. Biochem. 269 1259-1266 2002 FEBS 2002 Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein Edvards Liepinsh1 Gottfried Otting1 Margaret M. Harding2 Leanne G. Ward2 Joel P. Mackay3 and A. D. J. Haymet4 1Karolinska Institute Tomtebodavagen Stockholm Sweden 2School of Chemistry University of Sydney NSW Australia 3 Department of Biochemistry University of Sydney NSW Australia Department of Chemistry and Institute for Molecular Design University of Houston TX USA The solution structure of a synthetic mutant type I antifreeze protein AFP I was determined in aqueous solution at pH using nuclear magneiic resonanee NMIR spcctro-scopy. The mutations comprised the replacement of the four Thr residues by Val and the introduction of two additional Lys-Glu salt bridges. The antifreeze activity of this mutant peptide VVVV2KE has been previously shown to be similar to that of the wild type protein HPLC6 defined here as TTTT . The solution structure reveals an a helix bent in the same direction as the more bent conformer of the published crystal structure of TTTT while the side chain v I rotamers of VVVV2KE are similar to those of the straighter conformer in the crystal of TTTT. The Val side chains of VVVV2KE assume the same orientations as the Thr side chains of TTTT confirming the conservative nature of this mutation. The combined data suggest that AFP I undergoes an equilibrium between straight and bent helices in solution combined with independent equilibria between different side chain rotamers for some of the amino acid residues. The present study presents the first complete sequence-specific resonance assignments and the first complete solution structure determination by NMR of any AFP I protein. Keywords antifreeze a helices proteins winter flounder NMR spectroscopy. During the last two decades at least four classes of structurally diverse antifreeze or thermal hysteresis proteins type I-IV AFPs have been isolated from the serum

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