A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein ... View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999

AUTHORS

Christian Lücke , David Fushman , Christian Ludwig , James A. Hamilton , James C. Sacchettini , Heinz Rüterjans

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 usec-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. (Mol Cell Biochem 192: 109–121, 1999) More... »

PAGES

109-121

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-4929-1_13

DOI

http://dx.doi.org/10.1007/978-1-4615-4929-1_13

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036273690


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