Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein

W. Eberle, W. Klaus, G. Cesareni, C. Sander, P. Rosch

Research output: Contribution to journalArticle

Abstract

The complete resonance assignment of the Co1E1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3J(HNα) coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.

Original languageEnglish
Pages (from-to)7402-7407
Number of pages6
JournalBiochemistry
Volume29
Issue number32
DOIs
Publication statusPublished - 1990

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ASJC Scopus subject areas

  • Biochemistry

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