Literature DB >> 15631491

Polychromatic selective population inversion for TROSY experiments with large proteins.

Krystyna Bromek1, Donghan Lee, Richard Hauhart, Malgorzata Krych-Goldberg, John P Atkinson, Paul N Barlow, Konstantin Pervushin.   

Abstract

This paper presents polychromatic selective polarization inversion (PC-SPI) as an alternative to the polarization transfer methods recently developed for the application of NMR to large biological molecules. Theoretical and numerical considerations indicate that PC-SPI has the potential for more efficient polarization transfer under conditions of rapid transverse relaxation compared to J coupling- and cross-correlated relaxation-based transfers. The main advantage offered by the method presented here is the maintenance of near-optimal trajectories of inversion of the individual components of the spin magnetization while using broadband optimized pulses. A 2D experiment was implemented combining PC-SPI with TROSY-based chemical shift correlation. The experiment was applied to detect (15)N-(1)H chemical shift correlation spectra of a 200 kDa complex consisting of an 80% (2)H- and uniformly (15)N,(13)C-labeled 22 kDa portion of complement receptor type 1 and unlabeled C3b of complement (180 kDa).

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Year:  2005        PMID: 15631491     DOI: 10.1021/ja0462326

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  2 in total

1.  Multi-dimensional NMR without coherence transfer: minimizing losses in large systems.

Authors:  Yizhou Liu; James H Prestegard
Journal:  J Magn Reson       Date:  2011-07-21       Impact factor: 2.229

Review 2.  Site-specific labeling of proteins with NMR-active unnatural amino acids.

Authors:  David H Jones; Susan E Cellitti; Xueshi Hao; Qiong Zhang; Michael Jahnz; Daniel Summerer; Peter G Schultz; Tetsuo Uno; Bernhard H Geierstanger
Journal:  J Biomol NMR       Date:  2009-08-09       Impact factor: 2.835

  2 in total

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