Preprints  

Many NMR experiments need special broadband pulses to cover the needed radiofrequency bandwidth. Here we demonstrate the use of a pair of so-called SORDOR pulses that provide full hard pulse functionality at significantly lower rf-energy requirements as equivalent conventional pulse shapes. The pulses are characterized and their applicability in example experiments demonstrated.

Strong signals in Nuclear Magnetic Resonance are perturbed by their feedback interaction with the radio-frequency circuit, a phenomenon known as Radiation Damping . This effect is usually weak and influences solely the signals that are at its source. In this work, it is shown that, under certain circumstances, Radiation Damping can have far-reaching consequences.

Through the advent of fast magic-angle spinning and high magnetic fields, the spectral resolution of solid-state NMR spectra has recently been greatly improved. To take full advantage of this gain, the magnetic field must be stable over the experiment time of hours or even days. We thus monitor the field by simultaneous acquisition of a frequency reference (SAFR), and use this information to correct multidimensional spectra improving resolution and availability of productive magnet time.

This work provides some clarifications on the long known Redfield theory of spin relaxation, which considers a small system coupled to a large ensemble of particles in thermodynamic equilibrium. The derivation is rewritten so as to emphasize the usual assumptions and their consequences. In particular, the respective roles of the detailed balance balance assumption, as well as the non commutativity of the spin-bath coupling are discussed.

Providing evidence that proteins are dynamical molecules is a major contribution of solution NMR to structural biology. But the classical experiments to measure dynamics can only be applied to small proteins. This is regretful, because larger proteins often display conformational changes in which dynamics plays a functional role. We show here that dynamic information can be extracted from HSQC NMR spectra using a computational approach. Such spectra are widely available also for larger proteins.

We show here that information about protein molecular dynamics can be directly extracted out of a single NMR spectrum. Understanding protein dynamics is essential to understanding its function, energetics and biology. We hope that this contribution helps bring this insight to a much broader application field and audience community than previously possible.

The demonstration of the Finite Pulse Radio Frequency Driven Recoupling experiment was firstly published over the past 20 years. Since it has become one of the used experiments. In this article we consider that experiment using other theoretical and simulated approaches with respect to the previous works. These approaches help us to understand more clearly the influence of each part of that experiment and to see how exactly the spin system is evaluated during it.

We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. We asked whether a detailed analysis of the individual stability curves could provide additional site-specific information. By monitoring both cold and heat denaturation of individual residues we convincingly demonstrate that the two unfolding processes are intrinsically different.

Nowadays, almost all MRI technique used in clinical applications are based on a Fourier transformation of the raw data. Alternative non-Fourier magnetic resonance imaging techniques can offer some advantages under certain conditions. SPatio-temporal ENcoding (SPEN) is a non-Fourier method that usually employs frequency-swept radio frequency pulses and can give good images in inhomogeneous magnetic fields. In this work we show how one can improve this technique by using quadratic gradients.