A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding

Casagrande, F.; Ehler, A.; Burger, D.; Benz, J.; Ross, A.; Rudolph, M.G.

doi:10.1107/S2059798325006242

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
¹⁵N–¹H HSQC spectra of standard purified and delipidated hFABP4. (a) The heterogeneity of the standard purified FABP4 is reflected by poor resolution (broader peaks) and many additional spurious peaks throughout the spectrum, indicating several states of hFABP4. (b) After delipidation, i.e. the removal of fatty acids and other hydrophobic components by denaturation, hydrophobic chromatography and refolding, hFABP4 displays a highly homogenous ¹⁵N–¹H HSQC spectrum with fewer and well dispersed peaks. Blue and orange rectangles show enlargements of these spectral regions.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 8| August 2025| Pages 423-435

https://doi.org/10.1107/S2059798325006242

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