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.
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.
Lücke
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C
Institut für Biophysikalische Chemie, J.W. Goethe-Universität, Frankfurt, Germany.
Fushman
D
D
Ludwig
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C
Hamilton
J A
JA
Sacchettini
J C
JC
Rüterjans
H
H
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D002417:Cattle; D050556:Fatty Acid-Binding Proteins; D007082:Ileum / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D018996:Myelin P2 Protein / Q000737:chemistry*; D009206:Myocardium / Q000737:chemistry*; D009363:Neoplasm Proteins; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013552:Swine
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins