Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-12

AUTHORS

Meaghan E. Ward, Emily Ritz, Mumdooh A. M. Ahmed, Vladimir V. Bamm, George Harauz, Leonid S. Brown, Vladimir Ladizhansky

ABSTRACT

Direct proton detection is becoming an increasingly popular method for enhancing sensitivity in solid-state nuclear magnetic resonance spectroscopy. Generally, these experiments require extensive deuteration of the protein, fast magic angle spinning (MAS), or a combination of both. Here, we implement direct proton detection to selectively observe the mobile entities in fully-protonated membrane proteins at moderate MAS frequencies. We demonstrate this method on two proteins that exhibit different motional regimes. Myelin basic protein is an intrinsically-disordered, peripherally membrane-associated protein that is highly flexible, whereas Anabaena sensory rhodopsin is composed of seven rigid transmembrane α-helices connected by mobile loop regions. In both cases, we observe narrow proton linewidths and, on average, a 10× increase in sensitivity in 2D insensitive nuclear enhancement of polarization transfer-based HSQC experiments when proton detection is compared to carbon detection. We further show that our proton-detected experiments can be easily extended to three dimensions and used to build complete amino acid systems, including sidechain protons, and obtain inter-residue correlations. Additionally, we detect signals which do not correspond to amino acids, but rather to lipids and/or carbohydrates which interact strongly with membrane proteins. More... »

PAGES

375-388

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10858-015-9997-5

DOI

http://dx.doi.org/10.1007/s10858-015-9997-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022306535

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26494649


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