19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol.

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Article

19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol.

The Journal of biological chemistry - 15 Jul 1990

Li E, Qian S J, Yang N C, d'Avignon A, Gordon J I

Abstract excerpt

Rat cellular retinol binding protein (CRBP II) is a 134-amino acid intracellular protein synthesized in the polarized absorptive cells of the intestine. We have previously used 19F nuclear magnetic resonance (NMR) spectroscopy to survey the structural effects of ligand binding on the apoprotein. For these studies, all 4 Trp residues of rat CRBP II were efficiently labeled with 6-fluorotryptophan (6-F-Trp) by...

Topics

Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Escherichia coli
Fluorine
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Oligonucleotide Probes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Rats

Recombinant Proteins

Retinol-Binding Proteins

Retinol-Binding Proteins, Cellular

Tryptophan

Vitamin A

Source

Open in PubMed

Identifiers

PMID: 2195021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2195021-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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