Advances In Nuclear Magnetic Resonance Techniques Research Articles

Recent Advances in Solid-State Nuclear Magnetic Resonance Techniques for Materials Research

Establishing structure–property correlations is of paramount importance to materials research. The ability to selectively detect observable magnetization from transitions between quantized spin states of nuclei makes nuclear magnetic resonance (NMR) spectroscopy a powerful probe to characterize solids at the atomic level. In this article, we review recent advances in NMR techniques in six areas: spectral resolution, sensitivity, atomic correlations, ion dynamics, materials imaging, and hardware innovation. In particular, we focus on the applications of these techniques to materials research. Specific examples are given following the general introduction of each topic and technique to illustrate how they are applied. In conclusion, we suggest future directions for advanced solid-state NMR spectroscopy and imaging in interdisciplinary research.

Protein NMR spectroscopy: practical techniques and applications

Nuclear Magnetic Resonance (NMR) spectroscopy, a physical phenomenon based upon the magnetic properties of certain atomic nuclei, has found a wide range of applications in life sciences over recent decades. The dramatic advances in NMR techniques have led to corresponding advances in the ability of NMR to study the structure, dynamics and interactions of biological macromolecules in solution under close to physiological conditions. This volume focuses on the use of NMR to study proteins.

Protein dynamics from solution NMR: theory and applications.

Solution nuclear magnetic resonance (NMR) spectroscopy is unique in its ability to elucidate the details of atomic-level structural and dynamical properties of biological macromolecules under native-like conditions. Recent advances in NMR techniques and protein sample preparation now allow comprehensive investigation of protein dynamics over timescales ranging 14 orders of magnitude at nearly every atomic site. Thus, solution NMR is poised to reveal aspects of the physico-chemical properties that govern the ensemble distribution of protein conformers and the dynamics of their interconversion. We review these advances as well as their recent application to the study of proteins.