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In order to study the conformational stability induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough (DvH) cytochrome c 553 , fast peptic digestion of deuterated protein followed by separation and measurement of related peptides using liquid chromatography coupled to electro-spray ionization mass spectrometry was performed. We show that the H-bonding and/or...
Two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) was used to assign the proton resonances of ferricytochrome c 553 from Desulfovibrio vulgaris Hildenborough. The spin systems of 76 out of 79 amino acids were identified by J-correlation spectroscopy (COSY and HOHAHA) in H 2 O and D 2 O and correlated by nuclear Overhauser effect spectroscopy (NOESY)...
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