Publication | Closed Access
Proton Magnetic Resonance of Proteins Fully Deuterated except for <sup>1</sup> H-Leucine Side Chains
103
Citations
5
References
1968
Year
Protein ChemistryBiosynthesisBiotransformationLeucine Side ChainsBiochemistryMagnetic Resonance SpectroscopyProtein FoldingNatural SciencesMagnetic ResonanceMolecular BiologyProteins Fully DeuteratedCytochrome CProtein NmrMedicineProton Magnetic ResonanceProtein Biosynthesis
The fully deuterated proteins C-phycocyanin, C-phycoerythrin, and cytochrome c have been obtained by biosynthesis with the leucine side chains, and only the leucine side chains, of normal ((1)H) isotopic composition. In these (isotopic hybrid) proteins, proton magnetic resonance analysis shows that the (1)H-leucine side chains are in a variety of environments. During protein biosynthesis, the alpha hydrogen of leucine is exchanged with a hydrogen ((2)H) from the aqueous medium.
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