Off-resonance TROSY-selected R 1rho experiment with improved sensitivity for medium- and high-molecular-weight proteins. Academic Article

abstract

• NMR spin relaxation techniques that utilize relaxation interference phenomena (TROSY) enable chemical exchange processes to be characterized in high-molecular-weight proteins. A TROSY-selected (TS) approach for measuring off-resonance R1rho relaxation in the spin-locked rotating reference frame is developed using three principles: (i) deuteration of nonexchangeable 1H sites to minimize remote dipole-dipole interactions, (ii) selective excitation of the slowly relaxing 15N doublet component to obtain optimal initial conditions, and (iii) selective inversion of one of the 15N doublet components to suppress cross-relaxation during the spin-lock period. The method is validated using [90%-15N, 70%-2H] ubiquitin at 280 K. The TROSY-selected R1rho experiment enables characterization of backbone dynamics on the microsecond time scale in large proteins.

authors

• Igumenova, Tatyana

published proceedings

• J Am Chem Soc

author list (cited authors)

• Igumenova, T. I., & Palmer, A. G.

citation count

• 45

complete list of authors

• Igumenova, Tatyana I||Palmer, Arthur G

publication date

• June 2006

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Molecular Weight
• Nuclear Magnetic Resonance, Biomolecular
• Protein Conformation
• Proteins
• Sensitivity And Specificity
• Time Factors

PubMed Central ID

• 16787055

Digital Object Identifier (DOI)

• 10.1021/ja061692f

start page

• 8110

end page

• 8111

volume

• 128

issue

• 25

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja061692f