Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution. |
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Authors: | K S Bose R H Sarma |
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Affiliation: | Department of Chemistry State University of New York at Albany Albany, New York 12222 USA |
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Abstract: | The noise free 300 MHz 1H NMR spectra of β-DPN+, recorded in the Fourier mode at 12° and 68°C have been completely analysed by extensive computer simulation. It is shown, whether the coenzyme exists as an equilibrium mixture of folded ? extended forms (12°C) or in overwhelminghly extended forms (68°C), the backbone of both the nicotinamide and adenine fragments preferentially exist in conformation. This orientation is significantly different from those reported in the solid state for the extended species in contact with the enzyme where and orientations have been observed. It is suggested that specific interactions of the backbone with the various amino acid residues in the enzyme induces conformational aberrations in the backbone. Intimate details of the backbone conformation of the extended forms of AcPy-DPN+ and β-TPN+ are also presented. |
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