Ann E. McDermott

Bajaj

Barnes

Bauer

Boris Itin

Cheng

Cross

Fricke

Fritzsching

Gopinath

Gunther

Ivan V. Sergeyev

Loren A. Day

Ludwig

Palmer

Rivkah Rogawski

Rossini

Sergeyev

Siemer

Smith

Straus

Tsuboi

Vitzthum

Wenk

Yamamoto

Zagdoun

Significance
          This work presents a technique for dynamic nuclear polarization (DNP)-enhanced magic-angle spinning (MAS) solid-state NMR studies of complex proteins and biological assemblies. The sequential side-chain correlation approach streamlines the site-specific assignment of NMR peaks in multidimensional spectra, a critical step in determining structural information such as distances. When combined with DNP enhancement, fast MAS, and nonuniform sampling, this technique allows for faster data acquisition than previously possible. Applied to the intact Pf1 bacteriophage, sequential side-chain correlation spectra have enabled a virtually complete assignment using DNP data alone. These assignments shed insight into the chemical shift and linewidth changes associated with cryogenic temperatures. Our data point to hydration as a key variable influencing these parameters.</jats:p

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Proceedings of the National Academy of Sciences

Efficient assignment and NMR analysis of an intact virus using sequential side-chain correlations and DNP sensitization

Efficient assignment and NMR analysis of an intact virus using sequential side-chain correlations and DNP sensitization

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