OSA's Digital Library

Applied Spectroscopy

Applied Spectroscopy

| PUBLISHED BY SAS — AVAILABLE FROM SAS AND OSA

  • Vol. 24, Iss. 4 — Jul. 1, 1970
  • pp: 450–452

13C Nuclear Magnetic Resonance Spectra of Proteins

Paul C. Lauterbur

Applied Spectroscopy, Vol. 24, Issue 4, pp. 450-452 (1970)


View Full Text Article

Acrobat PDF (254 KB)





Browse Journals / Lookup Meetings

Browse by Journal and Year


   


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

Share
Citations
  • Export Citation/Save Click for help

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.

Citation
Paul C. Lauterbur, "13C Nuclear Magnetic Resonance Spectra of Proteins," Appl. Spectrosc. 24, 450-452 (1970)
http://www.opticsinfobase.org/as/abstract.cfm?URI=as-24-4-450


Sort:  Journal  |  Reset

References

References are not available for this paper.

Cited By

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited