Preprints  

We used NMR to sequentially assign the side chain resonances of the cytosolic domain of glycoprotein n of the Crimean-Congo hemorrhagic fever virus. The combination of cell-free protein synthesis with high-field NMR and artificial intelligence approaches made this possible in a time- and effort-efficient manner. Our results will be harnessed to study the membrane-bound form of the domain and its interactions with virulence factors, which will ultimately help to understand their role in disease.

Scalar couplings give rise to peak splitting in nuclear magnetic resonance (NMR) spectra. Couplings between atoms that span a rotatable bond report on the rotation angle of the bond. Here we describe a new computational method that can be used to analyze complex patterns of peak splitting. In addition to showing new ways of visualizing and analyzing the underlying data, we uncover how isolated parts of proteins behave differently than when they are embedded in a folded protein.

In our study, we correlate the first and the second harmonic detection modes of continuous wave electron paramagnetic resonance to identify metallic lithium traces present on the graphite anode after multi electrochemical cycles. Such metallic complexes are a source of limitations which reduces battery life and lead to serious safety issues. To improve their detection, we propose to record simultaneously the first and the second harmonic EPR spectrum.

To characterize the amplitude of dynamic processes in molecules, anisotropic parameters can be measured using solid-state NMR. However, it is not clear motions on which time scales lead to such a scaling of the anisotropic interactions. Using numerical simulations in small spin systems we could show that mostly the magnitude of the anisotropic interaction determines the range of time scales detected by the scaled anisotropic interaction and experimental parameters play a very minor role.

Drug discovery requires the testing of a large number of samples to identify molecules with a potential therapeutic potential. The recent development of methods to perform such tests within seconds using sample illumination in a magnetic field could increase the throughput of such studies. We present a setup that integrates light into fully automated and commercially available instrumentation. This platform upgrade can increase the drug discovery throughput by a factor of 20 to 50-fold.

We have written a programming library for biological NMR, a commonly used research method. Its use simplifies (makes it faster and less error-prone) development of new research methods. We demonstrate that it allows for consolidating several experimental methods into one file without adding complexity. We hope that it will be of use for other groups developing NMR experiments.

The magic angle spinning (MAS) technique of solid state NMR requires samples to be rapidly rotated within a magnetic field. The rotation rate speed record is 150 kHz, or 9 million RPM, and hence MAS turbines hold the world rotation speed record for extended objects. The containers holding the samples are made of the strongest materials known, to be able to withstand the excessive centrifugal forces. To overcome the speed limit, this paper delineates a way to do so using an optical tweezers setup

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.