A comparative study of the backbone dynamics of two closely related lipid binding proteins: bovine heart fatty acid binding protein and porcine ileal lipid binding protein. uri icon

abstract

  • The backbone dynamics of bovine heart fatty acid binding protein (H-FABP) and porcine ileal lipid binding protein (ILBP) were studied by 15N NMR relaxation (T1 and T2) and steady state heteronuclear 15N[1H] NOE measurements. The microdynamic parameters characterizing the backbone mobility were determined using the 'model-free' approach. For H-FABP, the non-terminal backbone amide groups display a rather compact protein structure of low flexibility. In contrast, for ILBP an increased number of backbone amide groups display unusually high internal mobility. Furthermore, the data indicate a higher degree of conformational exchange processes in the microsec-msec time range for ILBP compared to H-FABP. These results suggest significant differences in the conformational stability for these two structurally highly homologous members of the fatty acid binding protein family.

published proceedings

  • Mol Cell Biochem

author list (cited authors)

  • Lcke, C., Fushman, D., Ludwig, C., Hamilton, J. A., Sacchettini, J. C., & Rterjans, H.

citation count

  • 29

complete list of authors

  • Lücke, C||Fushman, D||Ludwig, C||Hamilton, JA||Sacchettini, JC||Rüterjans, H

publication date

  • February 1999