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Probing broad timescale and heterogeneous conformational dynamics in the catalytic core of the Arf-GAP ASAP1 via methyl adiabatic relaxation dispersion.

著者 Chao FA , Li Y , Zhang Y , Byrd RA
J Am Chem Soc.2019 Jul 11 ; ():.
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Methyl-TROSY is one of the most powerful NMR spectroscopic tools for studying structures and conformational dynamics of large protein complexes in solution. In studying conformational dynamics, side-chains usually display heterogeneous dynamics, including col-lective and local motions, that can be difficult to detect and analyze by conventional relaxation dispersion (RD) approaches. The combi-nation of NH-based adiabatic relaxation dispersion experiments and geometric approximation (geoHARD) has been shown to have sev-eral advantages over conventional RD to reveal conformational dynamics over a broad timescale. Here, we demonstrate a new technique developed to detect both heterogeneous and wide timescale conformational dynamics in the hydrophobic interior of large macro-molecules utilizing methyl-geoHARD. It is shown that methyl-geoHARD will be feasible at ultra-high magnetic fields (> 1 GHz), when this technology becomes available. For the ZA domain of the Arf-GAP ASAP1, with a global correlational time of 24 ns at 15 ˚C, a wide range of conformational dynamics (exhibiting chemical exchange (kex) values between 0.1~100 k s-1) is observed in the methyl groups of isoleucine, leucine, and valine. The dynamics include collective and independent local motions. Furthermore, portions of the collective motions have been confirmed by single-quantum Carr-Purcell-Meiboom-Gill (SQ-CPMG) RD experiments; however, motions outside of the detectable CPMG window (400-8000 s-1) cannot be accurately determined by SQ-CPMG experiments. The methyl-geoHARD experiment allows dissection of heterogeneous conformational dynamics and pinpoints important motions that, potentially, can be correlated with important biological functions and recognition.
PMID: 31293161 [PubMed - as supplied by publisher]
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