English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In recent years, there has been a growing interest in fast acquisition and analysis of nuclear magnetic resonance (NMR) spectroscopy data for high throughput protein structure determination. Towards this end, rapid data collection techniques and methods to simplify the NMR spectrum such as amino acid selective unlabeling have been proposed recently. Combining these two approaches can speed up further the structure determination process. Based on this idea, we present three new two-dimensional (2D) NMR experiments, which together provide 15N, 1HN, 13Cα, 13Cβ, 13C′ chemical shifts for amino acid residues which are immediate C-terminal neighbors (i + 1) of residues that are selectively unlabeled. These experiments have high sensitivity and can be acquired rapidly using the methodology of G-matrix Fourier transform (GFT) NMR spectroscopy combined with non-uniform sampling (NUS). This is a first study involving the application of fast NMR methods to proteins samples prepared using a specific labeling scheme. Taken together, this opens up new avenues to using the method of selective unlabeling for rapid resonance assignment of proteins

Accelerating NMR-Based Structural Studies of Proteins by Combining Amino Acid Selective Unlabeling and Fast NMR Methods