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Default Measurement of amide proton chemical shift anisotropy in perdeuterated proteins using CSA amplification

Measurement of amide proton chemical shift anisotropy in perdeuterated proteins using CSA amplification

Publication date: Available online 19 September 2017
Source:Journal of Magnetic Resonance

Author(s): Yuwei Ge, Ivan Hung, Xiaoli Liu, Maili Liu, Zhehong Gan, Conggang Li

Measuring 1H chemical shift anisotropy (CSA) is useful for probing proton environments and dynamics but remains a challenge due to strong homonuclear interaction and relatively small shift anisotropy, especially in proteins with multiple proton sites. Here the extended chemical shift anisotropy amplification (xCSA) method is applied for amide proton CSA measurement in uniformly 2H enriched proteins under fast magic angle spinning. The xCSA method is capable of distinguishing the sign of the CSA asymmetry parameter, complimenting other multiple-pulse recoupling methods. A three-dimensional xCSA experiment is demonstrated for measuring the proton CSA of amide sites in a GB1 protein sample and the possible correlation of amide proton CSA with protein secondary structure is discussed.
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