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Structure‐function relationship in Escherichia coli translational initiation factors Characterization of IF1 by high‐resolution 1 H‐NMR spectroscopy
Author(s) -
Paci Maurizio,
Pon Cynthia L.,
Gualerzi Claudio O.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80042-5
Subject(s) - nuclear magnetic resonance spectroscopy , chemistry , spectroscopy , escherichia coli , relaxation (psychology) , transverse relaxation optimized spectroscopy , crystallography , spin–lattice relaxation , protein structure , site directed spin labeling , resonance (particle physics) , nuclear magnetic resonance , stereochemistry , fluorine 19 nmr , biochemistry , physics , biology , quantum mechanics , neuroscience , nuclear quadrupole resonance , gene , particle physics , membrane
Escherichia coli translational initiation factor IF1 was studied by 1 H‐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.