13C Nuclear Magnetic Resonance Spectra of Proteins

Author:

Lauterbur Paul C.1

Affiliation:

1. Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11790

Abstract

Although 13C has a natural abundance of only 1.1% and gives inherently much weaker nuclear magnetic resonance signals than does does 1H, it has been found that 13C nuclear magnetic resonance spectra of aqueous solutions of naturally occurring proteins can be observed. A spectrum of hen's egg white lysozyme, an enzyme of molecular weight approximately 14 300, containing 129 amino acid residues, has been partially analyzed by comparison with a computer—simulated spectrum.

Publisher

SAGE Publications

Subject

Spectroscopy,Instrumentation

Cited by 38 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Lauterbur, Paul C.: One Path out of Many-How MRI Actually Began;Encyclopedia of Magnetic Resonance;2007-03-15

2. The Development of NMR;Encyclopedia of Magnetic Resonance;2007-03-15

3. The detection of mercury, lead, and methylmercury binding sites on lysozyme by carbon-13 NMR chemical shifts of the carboxylate groups;Journal of Inorganic Biochemistry;1988-04

4. Humic substances: Part structural aspects;Toxicological & Environmental Chemistry;1981-12

5. Nuclear Magnetic Resonance of Biological Samples;C R C Critical Reviews in Analytical Chemistry;1981-01

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