Solid-state NMR and protein dynamics

Krushelnitsky, Alexey; Reichert, Detlef

doi:10.1016/j.pnmrs.2005.04.001

Cited by 102 publications

(72 citation statements)

References 130 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The analytical averaging over the MAS rotation (which is usually allowed because the relaxation time is much longer than the rotor period) leads to a simplified correlation function of the form (26) If the correlation function of the internal motion is diagonal, i.e., if the correlation function is zero for p ≠ p' then the total correlation function and, therefore, also the relaxation-rate constant is independent of the α MR angle of the powder average and it is sufficient to average over the angle β MR . Therefore, the correlation function becomes even simpler in this case and we end up with (27) Based on the derivation of the master equation of relaxation (see Eq.…”

Section: Relaxation In Solidsmentioning

confidence: 99%

See 1 more Smart Citation

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

189

295

View full text Add to dashboard Cite

Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR, with an emphasis on the underlying theoretical concepts and differences of MAS solid-state NMR compared to solution-state NMR. The theoretical foundations of nuclear spin relaxation are revisited, focusing on the particularities of spin relaxation in solid samples under magic-angle spinning. We discuss the range of validity of Redfield theory, as well as the inherent multi-exponential behavior of relaxation in solids. Experimental challenges for measuring relaxation parameters in MAS solid-state NMR and a few recently proposed relaxation approaches are discussed, which provide information about time scales and amplitudes of motions ranging from picoseconds to milliseconds. We also discuss the theoretical basis and experimental measurements of anisotropic interactions (chemical-shift anisotropies, dipolar and quadrupolar couplings), which give direct information about the amplitude of motions. The potential of combining relaxation data with such measurements of dynamically-averaged anisotropic interactions is discussed. Although the focus of this review is on the theoretical foundations of dynamics studies rather than their application, we close by discussing a small number of recent dynamics studies, where the dynamic properties of proteins in crystals are compared to those in solution.

show abstract

Section: Relaxation In Solidsmentioning

confidence: 99%

“…These approaches, (for biomolecules in particular deuterium-based experiments), have been reviewed elsewhere [19][20][21][22][23]. For additional complementary views of (bio-)molecular dynamics studied by solution-or solid-state NMR spectroscopy, we refer the reader to existing reviews [3,5,[23][24][25][26][27][28][29][30]]. …”

Section: Introductionmentioning

confidence: 99%

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

189

295

View full text Add to dashboard Cite

show abstract

“…The dynamics evolves on a multidimensional energy landscape with various interactions and conformations over wide time-and length scales [2][3][4][5][6]. Figure 1 shows typical time scales of biologically relevant motions involved in protein dynamics and enzyme actions, covering 15 orders of magnitude of temporal evolution from femtosecond to second [1,4,[7][8][9][10]. For a typical enzymatic function, the catalytic process can be a series of elementary chemical reactions such as proton transfer and electron transfer, occurring on the ultrafast time scale of less than nanosecond.…”

Section: Introductionmentioning

confidence: 99%

Femtochemistry in enzyme catalysis: DNA photolyase

Kao

Saxena

Wang

et al. 2007

Cell Biochem Biophys

View full text Add to dashboard Cite

Photolyase uses light energy to split UV-induced cyclobutane pyrimidine dimers in damaged DNA. This photoenzyme encompasses a series of elementary dynamical processes during repair function from early photoinitiation by a photoantenna molecule to enhance repair efficiency, to in vitro photoreduction through aromatic residues to reconvert the cofactor to the active form, and to final photorepair to fix damaged DNA. The corresponding series of dynamics include resonance energy transfer, intraprotein electron transfer, and intermolecular electron transfer, bond breaking-making rearrangements and back electron return, respectively. We review here our recent direct studies of these dynamical processes in real time, which showed that all these elementary reactions in the enzyme occur within subnanosecond timescale. Active-site solvation was observed to play a critical role in the continuous modulation of catalytic reactions. As a model system for enzyme catalysis, we isolated the enzyme-substrate complex in the transition-state region and mapped out the entire evolution of unmasked catalytic reactions of DNA repair. These observed synergistic motions in the active site reveal a perfect correlation of structural integrity and dynamical locality to ensure maximum repair efficiency on the ultrafast time scale.

show abstract

“…In our case of moderate solvation levels, proteins, including elastin, are expected to exhibit anisotropic internal dynamics [37][38][39][44][45][46]. 13 C CP MAS NMR spectra provide valuable information about such fluctuations [35,47].…”

Section: Methodical Aspectsmentioning

confidence: 99%