Organic Magnetic Resonance 2007-12-01

Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples.

Zhaoxiong Zheng, Wei Qiang, David P Weliky

Index: Magn. Reson. Chem. 45 Suppl 1 , S247-60, (2007)

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Abstract

Two finite-pulse radiofrequency-driven recoupling (RFDR) methods were compared and applied to the measurement of 3-6 Å (13)CO-(13)CO distances in polycrystalline and membrane-associated HIV fusion peptide (HFP) samples. The RFDR methods were based on π pulses and were relatively straightforward to implement and insensitive to pulse imperfections. The two tested methods were: (i) constant-time double-quantum buildup with finite pulses (fpCTDQBU) for which the pulse sequence maintained a constant transverse relaxation period while allowing a variable period of dipolar dephasing; and (ii) constant-time finite-pulse rf-driven recoupling (fpRFDR-CT) for which the duration of transverse relaxation increased with increasing dephasing period. The fpRFDR-CT method yielded higher signal-to-noise and an accurate determination of a ~5 Å intercarbonyl distance was made in a crystalline peptide which had T(2) ≈ 55 ms. In some contrast, the HFP samples had T(2) ≈ 15 ms and the fpRFDR-CT data were dominated by transverse relaxation. Examination of the fpCTDQBU sequence showed: (i) the most rapid signal buildup was obtained with application of one (13) C π pulse per rotor period rather than one (13)C π pulse per multiple rotor periods and (ii) the data were insensitive to ~15 ppm transmitter offset and to ~5° variation of π pulse nutation angle. For HFP samples which were (13)CO labeled at a single residue, analyses of the fpCTDQBU data were interpreted with a model of mixed parallel and antiparallel β-strand arrangements in the N-terminal region of HFP and loss of parallel β-sheet structure in the C-terminal region of HFP.Copyright © 2007 John Wiley & Sons, Ltd.