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

Mol Cell Biochem. 1999 Feb;192(1-2):109-21.

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.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Carrier Proteins / chemistry*
  • Cattle
  • Fatty Acid-Binding Proteins
  • Ileum / chemistry*
  • Magnetic Resonance Spectroscopy
  • Myelin P2 Protein / chemistry*
  • Myocardium / chemistry*
  • Neoplasm Proteins*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Swine

Substances

  • Carrier Proteins
  • Fatty Acid-Binding Proteins
  • Myelin P2 Protein
  • Neoplasm Proteins