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

doi:10.1021/bi00484a007

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

Fondazione Santa Lucia

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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 language	English
Pages (from-to)	7402-7407
Number of pages	6
Journal	Biochemistry
Volume	29
Issue number	32
DOIs	https://doi.org/10.1021/bi00484a007
Publication status	Published - 1990

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Biochemistry

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Eberle, W., Klaus, W., Cesareni, G., Sander, C., & Rosch, P. (1990). Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein. Biochemistry, 29(32), 7402-7407. https://doi.org/10.1021/bi00484a007

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T1 - Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein

AU - Eberle, W.

AU - Klaus, W.

AU - Cesareni, G.

AU - Sander, C.

AU - Rosch, P.

PY - 1990

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AB - 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.

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10.1021/bi00484a007