1                                              ILBP had an intermediate state with molten globule-like

2                                              ILBP was less stable than IFABP with a midpoint of 2.9 M

3                                              ILBPs from different species show high sequence and stru

4 proteins, two mutations (F68C-IFABP and C69F-ILBP) were made that swapped a more hydrophobic residue

5 nativelike secondary structure, whereas C69F-ILBP followed an unfolding path that was identical to th

6 siological conditions the mutant (Deltaalpha-ILBP) is highly disordered.

7 sition in both proteins (F93S-IFABP and F94S-ILBP).

8                                        Human ILBP binds bile acid derivatives in a well-characterised

9  similar, with 123 of the 127 amino acids of ILBP having backbone and C(beta) conformations nearly id

10 nding proteins, ileal lipid binding protein (ILBP) and intestinal fatty acid binding protein (IFABP),

11  homologous rat ileal lipid binding protein (ILBP) displays an intermediate during unfolding with nat

12  (ASBT) and the ileal lipid-binding protein (ILBP) were assessed by Western blotting with quantitatio

13 ABP (intestinal fatty acid-binding protein), ILBP (ileal fatty acid-binding protein), CRABP I (cellul

14  intracellular ileal lipid binding proteins (ILBPs) are involved in the transport and enterohepatic c

15 r, we show that the highly homologous rabbit ILBP (82% sequence identity) with seven conservative sub

16 unction or the expression of the ASBT or the ILBP.

17 ed an unfolding path identical to that of WT-ILBP with an intermediate that showed nativelike seconda