Homo-nuclear 13C J-decoupling in uniformly 13C-enriched solid proteins. Academic Article

abstract

• Recently, we reported an analysis of carbon lineshapes in high resolution solid-state NMR spectra of uniformly 13C-enriched amino acids. Application of a 13C J-decoupling protocol during the carbon chemical shift evolution period allowed us to separate the contribution of the second-order dipolar shift from that of the 13C-13C J-coupling interactions to carbon linewidths. In this work, we have extended this approach to microcrystalline proteins. We describe the performance of the J-decoupling sequence applied to remove homo-nuclear 13C J-couplings in the 13C spectra of ubiquitin. Analysis of the J-decoupling efficiency for C(alpha) and carbonyl protein sites showed that a significant gain in resolution can be achieved.

authors

• Igumenova, Tatyana

published proceedings

• J Magn Reson

author list (cited authors)

• Igumenova, T. I., & McDermott, A. E.

citation count

• 17

complete list of authors

• Igumenova, Tatyana I||McDermott, Ann E

publication date

• July 2005

publisher

• Elsevier  Publisher

published in

• Journal of Magnetic Resonance  Journal

keywords

• Algorithms
• Amino Acids
• Carbon Isotopes
• Magnetic Resonance Spectroscopy
• Proteins
• Ubiquitin

PubMed Central ID

• 15949744

Digital Object Identifier (DOI)

• 10.1016/j.jmr.2005.03.007

start page

• 11

end page

• 20

volume

• 175

issue

• 1

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.jmr.2005.03.007