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Journal Article

Proton Magnetic Resonance of Proteins Fully Deuterated except for $^{1}$H-Leucine Side Chains

Henry L. Crespi, Robert M. Rosenberg and Joseph J. Katz
Science
New Series, Vol. 161, No. 3843 (Aug. 23, 1968), pp. 795-796
Stable URL: http://www.jstor.org/stable/1725800
Page Count: 2

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Topics: Proton magnetic resonance, Amino acids, Hydrogen, Cytochromes, Hybridity, Protons, Biochemistry, Acetates
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Abstract

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) side chains are in a variety of environments. During protein biosynthesis, the alpha hydrogen of leucine is exchanged with a hydrogen $^{1}$H-leucine from the aqueous medium.

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