Distribution of Pico- and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation
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The transverse relaxation rates R (2) = 1/T (2) of protons can be determined by spin-echo sequences with multiple refocusing pulses using moderate radio-frequency field strengths and properly chosen inter-pulse delays so as to suppress echo modulations due ...
A model for calculating the influence of anisotropic collective motions on NMR relaxation rates in crystalline proteins is presented. We show that small-amplitude (
Engrailed 2 is a transcription factor belonging to the class of homeoproteins. These proteins possess a 60-residue DNA binding globular domain and play an important role in the early stages of development. We expressed and purified a 13.4 kDa fragment of E ...
Nuclear magnetic resonance is used to investigate the backbone dynamics in 6-phosphogluconolactonase from Trypanosoma brucei (Tb6PGL) with (holo-) and without (apo-) 6-phosphogluconic acid as ligand. Relaxation data were analyzed using the model-free appro ...
Relaxation processes induced by the antisymmetric part of the chemical shift anisotropy tensor (henceforth called anti-CSA) are usually neglected in NMR relaxation studies. It is shown here that anti-CSA components contribute to longitudinal relaxation rat ...
We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion ...
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to ob ...
Slow dynamic processes, such as biomolecular folding/unfolding, macromolecular diffusion, etc., can be conveniently monitored by solution-state two-dimensional (2D) NMR spectroscopy, provided the inverse of their rate constants does not exceed the nuclear ...
Multiple quantum relaxation in proteins reveals unexpected relationships between correlated or anti-correlated conformational backbone dynamics in alpha-helices or beta-sheets. The contributions of conformational exchange to the relaxation rates of C'N coh ...
Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross ...