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- W4366609295 abstract "NMR-based structural biology is an outstanding approach to understand the structure dynamics-function paradigm of biomacromolecules at atomic resolution and near physiological conditions. Various multidimensional NMR methods described in the previous chapters allowed the structural and dynamic studies of small proteins with size up to ˜30 kDa. However, in the case of larger molecules, the faster relaxation of resonances leads to line broadening and poor spectral sensitivity. NMR methods were developed devoting to extend the applications of solution NMR to larger molecular systems. Introduction of transverse relaxation-optimized spectroscopy (TROSY) in combination with various isotope-labeling techniques opened avenues to study very large biomacromolecules. In this Chapter, we describe the concepts of TROSY, theoretical principles and important recent applications in structural and functional studies of large biological macromolecules. We further describe various highly efficient polarization transfer methods such as cross-correlated relaxation-enhanced polarization transfer (CRINEPT) and cross-correlated relaxation-induced polarization transfer (CRIPT), which allowed the application of TROSY for molecular weights above 200 kDa up to ˜1MDa size. Selected important applications of TROSY-based experiments are discussed in this chapter. The TROSY scheme is sufficient to perform detailed studies on NMR resonance assignment, intermolecular interactions, structural investigation and dynamic processes." @default.
- W4366609295 created "2023-04-23" @default.
- W4366609295 creator A5056467612 @default.
- W4366609295 creator A5084176856 @default.
- W4366609295 date "2023-04-14" @default.
- W4366609295 modified "2023-10-02" @default.
- W4366609295 title "<scp>TROSY</scp>" @default.
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