The interactions of retinoids with retinol-binding protein. A resonance Raman spectroscopic study.
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 interaction 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.
Manor
D
D
Department of Physics, City College of the City University of New York, NY.
Callender
R
R
Noy
N
N
D005030:Ethylenes / Q000737:chemistry; D006860:Hydrogen Bonding; D012176:Retinoids / Q000737:chemistry*; D012177:Retinol-Binding Proteins / Q000737:chemistry*; D013059:Spectrum Analysis, Raman
D005030:Ethylenes; D012176:Retinoids; D012177:Retinol-Binding Proteins; C036216:ethylene