Structure‐function relationship in Escherichia coli translational initiation factors Characterization of IF1 by high‐resolution 1H‐NMR spectroscopy
- 29 August 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 236 (2) , 303-308
- https://doi.org/10.1016/0014-5793(88)80042-5
Abstract
Escherichia coli translational initiation factor IF1 was studied by 1H‐NMR spectroscopy at 400 MHz. IF1 displays a very well resolved spectrum in both aromatic and aliphatic regions. Other spectral characteristics include relatively narrow resonance lines and lack of relevant cross‐relaxation phenomena. The resonances of the aromatic residues, in particular of the two His and two Tyr, were assigned by selective chemical modifications and spectroscopic techniques to individual residues in the protein sequence. The relative mobility of various residues of IF1 has been evaluated on the basis of the spin‐lattice relaxation times which are rather short and homogeneous. Overall the factor appears to have a complex secondary and tertiary structure and to be a flexible protein whose residues have a high degree of internal mobility.Keywords
This publication has 12 references indexed in Scilit:
- Chemical synthesis and in vivo hyperexpression of a modular gene coding for Escherichia coli translational initiation factor IF1Molecular Genetics and Genomics, 1987
- Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNANature, 1986
- Mechanism of protein biosynthesis in prokaryotic cellsFEBS Letters, 1984
- Effect of Escherichia coli initiation factors on the kinetics of N-AcPhe-tRNAPhe binding to 30S ribosomal subunits. A fluorescence stopped-flow studyBiochemistry, 1983
- Structure‐function relationships in Escherichia coliinitiation factorsFEBS Letters, 1979
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979
- The Application of High Resolution Nuclear Magnetic Resonance to Biological SystemsPublished by Wiley ,1979
- Proton magnetic relaxation and spin diffusion in proteinsJournal of Magnetic Resonance (1969), 1976
- Complete tyrosine assignments in the high field proton nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitorBiochemistry, 1975
- Studies on the in vitro synthesis of β-galactosidase: Necessary components in the ribosomal washArchives of Biochemistry and Biophysics, 1974