Article
Mechanism of ligand-induced folding of a natively unfolded helixless variant of rabbit I-BABP.
Biochemistry - 11 Aug 2009
Rea Anita M, Thurston Victoria, Searle Mark S
Abstract excerpt
Substitution of the helix-turn-helix capping motif (residues 9-35) of rabbit I-BABP with a flexible Gly-Gly-Ser-Gly linker results in the loss of stabilizing hydrophobic contacts and renders the beta-clamshell structure of this steroidal bile acid transport protein unfolded. However, in the presence of a bile acid ligand, we observe strong coupling between binding and folding, resulting in an enthalpy-driven...
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