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

Molecular and Cellular Biochemistry - Tập 192 - Trang 109-121 - 1999
Christian Lücke1, David Fushman2, Christian Ludwig1, James A. Hamilton3, James C. Sacchettini4, Heinz Rüterjans1
1Institut für Biophysikalische Chemie, J.W. Goethe-Universität, Frankfurt, Germany
2The Rockefeller University, New York, USA
3Department of Biophysics, Boston University School of Medicine, Boston, USA
4Department of Biochemistry and Biophysics, Texas A&M University, College Station, USA

Tóm tắt

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 μsec-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.

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