Structure‐function relationship in Escherichia coli translational initiation factors Characterization of IF1 by high‐resolution 1H‐NMR spectroscopy

FEBS Letters

Gualerzi, Claudio O.¹  Pon, Cynthia L.¹  Paci, Maurizio² 

[1] Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, D-1000 Berlin 33, Germany;Department of Chemical Science and Technology, University of Rome, Tor Vergata, I-001 Rome, Italy

关键词: Translation;    Initiation factor 1;    1H-NMR;    Relaxation time;    Protein structure;   

DOI  :  10.1016/0014-5793(88)80042-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown