The interactions of retinoids with retinol-binding protein. A resonance Raman spectroscopic study

D. Manor, Robert Callender, N. Noy

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)413-418
Number of pages6
JournalEuropean Journal of Biochemistry
Volume213
Issue number1
StatePublished - 1993
Externally publishedYes

Fingerprint

Polyenes
Retinol-Binding Proteins
Retinoids
Hydrogen Bonding
Tretinoin
Vitamin A
Raman scattering
Hydrogen bonds
Oxygen
Water
Serum
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The interactions of retinoids with retinol-binding protein. A resonance Raman spectroscopic study. / Manor, D.; Callender, Robert; Noy, N.

In: European Journal of Biochemistry, Vol. 213, No. 1, 1993, p. 413-418.

Research output: Contribution to journalArticle

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