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

Pub. Date : 1994 Jan 15

PMID : 8307026






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy. Hydrogen leghemoglobin A Glycine max
2 Homonuclear two-dimensional and three-dimensional 1H-NMR spectroscopy has been utilized to study the 15.9-kDa protein soybean leghemoglobin. Hydrogen leghemoglobin A Glycine max
3 The secondary structure of leghemoglobin in solution has been determined on the basis of NOE connectivity patterns, hydrogen exchange and chemical-shift analyses. Hydrogen leghemoglobin A Glycine max
4 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. Hydrogen leghemoglobin A Glycine max