We have measured the pre‐resonance Raman spectrum of retinal, retinoic acid and retinol in dilute CCl4 solutions and when bound to the bovine‐serum retinol‐binding protein. The comparison reveals that the binding interactions does not involve any specific interactions of the head group and/or the polyene chain with a particular protein residue. The data indicate hydrogen bonding of bound retinal's head‐group oxygen to water, as well as some torsional angle change of its polyene chain upon binding.
|Number of pages
|European Journal of Biochemistry
|Published - Apr 1993
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