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Default 1H resonance assignments and secondary structure of the carbon monoxide complex of so

1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy.

Related Articles 1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy.

Eur J Biochem. 1994 Jan 15;219(1-2):611-26

Authors: Morikis D, Lepre CA, Wright PE

Homonuclear two-dimensional and three-dimensional 1H-NMR spectroscopy has been utilized to study the 15.9-kDa protein soybean leghemoglobin. NMR experiments were performed on the diamagnetic carbon monoxide complex at two temperatures and two pH values. Sequence-specific assignments have been made for 94% of the backbone and approximately 70% of the expected side-chain resonances. The secondary structure of leghemoglobin in solution has been determined on the basis of NOE connectivity patterns, hydrogen exchange and chemical-shift analyses. Leghemoglobin consists of seven helices and, unlike mammalian myoglobins, is missing the D helix. Instead an extended loop, the CE loop, is observed which might have importance for ligand entry into and exit from the protein interior. The hydrogen exchange behavior for the F helix and at the beginning of the A helix suggests different dynamic stability compared to other helical regions in leghemoglobin. Population of a second protein conformation, in which there is perturbation at the A-G-H helix interface, is observed at low pH.

PMID: 8307026 [PubMed - indexed for MEDLINE]



Source: PubMed
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