Membrane proteins are the next frontier for structural biology. It is feasible to determine the structures of smaller membrane proteins in micelles with solution NMR methods. However, it is the ability of solid-state NMR experiments to give completely resolved spectra of immobile proteins that enables the structures of larger membrane proteins to be determined in the definitive environment of lipid bilayers.
With the ability to determine atomic resolution structures of biological macromolecules in semi-physiological conditions, nuclear magnetic resonance spectroscopy (NMR) has become an eminent tool in structural biology. NMR provides a means for studying critical biological phenomena including protein structure, dynamics and folding as well as a practical approach to drug design.
A growing understanding of the diversity of structures and biological functions of DNA and RNA, coupled with progress in synthetic and spectroscopic techniques, have allowed remarkable progress in NMR studies of nucleic acids. Here we review novel principles of nucleic acid structure and recognition revealed by these studies and highlight opportunities for future progress.
The combination of stable isotope labelling and advanced multinuclear NMR technologies has opened up new avenues for the structural determination of biological macromolecules.
X-ray crystallography and nuclear magnetic resonance spectroscopy are not competing techniques, but rather they complement each other. Taken together they can provide an atomic detail picture of macromolecular structure and dynamics which can be used to obtain an understanding of life processes at the molecular level.
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.
京公网安备 11010802042870号
京ICP备2023020795号-1
扫码关注我们
求助内容：
应助结果提醒方式：