Principles and applications of cross-correlated relaxation in biomolecules

Brutscher, Bernhard

doi:10.1002/1099-0534(2000)12:4<207::aid-cmr3>3.0.co;2-c

Cited by 67 publications

(50 citation statements)

References 48 publications

(12 reference statements)

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“…In this section we review two recently proposed approaches, namely relaxation due to correlation of a dipolar and a CSA interaction, and cross-correlated relaxation due to interference of two chemical-shift tensors. In principle, additional cross-correlated relaxation rates could be exploited to study dynamics, such as dipole-dipole cross-correlated relaxation, which have been used in solution state [115][116][117][118][119] but, to our knowledge, this has not yet been implemented experimentally.…”

Section: 3mentioning

confidence: 99%

“…In this case, interference of the 15 [115,116]. The differential relaxation of the two components arises because the relaxation of one component is given by the sum of the two relaxation contributions, i.e.…”

Section: Csa/dipole Interferencementioning

confidence: 99%

“…This effect, which is known in solution-state NMR as "transverse-relaxation optimized spectroscopy" (TROSY) [124] effect has first been reported in solids by Chevelkov and Reif [112,125]. For solution-state NMR, these crosscorrelated relaxation effects can be fully described within the framework of Redfield theory, and they have been extensively reviewed [115,116,126]. Due to the absence of overall tumbling, the dependence of the CSA/D CCR on the motional parameters in MAS solidstate NMR is different from what is observed in solution, and we investigate the properties of the differential relaxation in the following briefly.…”

Section: Csa/dipole Interferencementioning

confidence: 99%

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

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

190

295

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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.

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Section: 3mentioning

confidence: 99%

Section: Csa/dipole Interferencementioning

confidence: 99%

Section: Csa/dipole Interferencementioning

confidence: 99%

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

Schanda

Ernst

2016

Progress in Nuclear Magnetic Resonance Spectroscopy

190

295

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“…This methodology is called J-scaled TROSY or J-enhanced (JE) TROSY. 41,43,44 A related J-scaling procedure was introduced to the 3D experiment using a 2 H/ 15 N/ 13 C labeled protein, 3D TROSY-HNCO, which introduces a third 13 C dimension so as to avoid resonance overlap in recording scaled-and native-TROSY 15 N chemical shifts. 41 Experiments were applied to proteins over 50 kDa.…”

Section: Data Acquisition Of the Rdcmentioning

confidence: 99%

Anisotropic Nuclear Spin Interactions for the Morphology Analysis of Proteins in Solution by NMR Spectroscopy

Tate

2008

ANAL. SCI.

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NMR spectroscopy has become a standard method to determine the high-resolution structure of biomolecules, including protein, nucleic acids and their complexes.Conventional NMR structural determination is based on distance restraints obtained from proton-proton nuclear Overhauser effects (NOEs), which give approximate distances between interacting protons close together in space (< 5 -6 Å), and the torsion angles through vicinal spin couplings. 1 These NMR parameters all give shortrange structural information.Although the observable maximum distance by NOEs is limited, basically less than 5 Å, the short-range structural constraints can connect parts of a molecule that are far apart in the primary sequence, but close together in the three-dimensional coordinate of a globular protein. In this way, the short-range structural constraints successfully allowed accurate determination of secondary and tertiary molecular geometry of globular proteins.1 In spite of the great success of conventional NMR for the structural determination of globular proteins, there are significant limitations in determining multidomain protein structures that possess a hinge region situated between domains. In such cases, the number of proton distances may be insufficient to define the spatial arrangement of the respective domains. Furthermore, the NOE-derived distance restraints have limited accuracy; the parts defined by the sparse NOE interactions are not fully reliable. Thus, the relative positions of distant parts of extended or modular proteins are often poorly defined.In many multidomain proteins, the relative orientation of domains change in response to ligand binding or covalent modification, which includes phosphorylation, acetylation, methylation and so forth. Agency,[3][4][5] Chiyoda, Japan Determining the relative orientation of domains within a protein is an important problem in structural biology, which has been difficult to address by either X-ray crystallography or NMR. The structure of a multidomain protein in a crystal lattice can be altered by crystal packing forces, resulting in different domain arrangements from those in solution. On the other hand, conventional NMR primarily provides short-range structural information, including proton-proton distances derived from nuclear Overhauser effects (NOEs) and torsion angles through vicinal spin couplings. Thus, NMR cannot always determine the precise interdomain arrangements due to the sparsely observed spin interactions between domains. However, the weak alignment of proteins in solution has enabled a new NMR technique to determine the domain arrangement based on the different structural information, which defines the orientation of a structural unit in protein against the magnetic field. This technique relies on the anisotropic nuclear spin interactions that only occur for a molecule in a weakly aligned state. In this review, the basics of the new NMR approach are described with focusing on its application to domain orientation analysis. We also describe our recently est...

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“…Both correlated and uncorrelated motions are possible [4,5]. Corretated motions have been recently investigated with a variety of nuclear magnetic resonance (NMR) techniques [5][6][7][8][9][10]. It is interesting to study the change in intemal dynamics under the influence of various perturbations.…”

Section: Introductionmentioning

confidence: 95%

Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates

Vugmeyster

Bodenhausen

2005

Appl. Magn. Reson.

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The temperature dependence of nuclear magnetic resonance relaxation rates was investigated for the backbone of tSN/~3C labeled human ubiquitin in the temperature range of 20-50 ~ The ~SN autorelaxation rates give evidente that the potential energy functions for ~SN-HN bonds ate not quadratic, in agreement with results for other proteins. Cross-correlation rates arising from correlated fluctuations of two ~SN-HN dipole~iipole interactions involving successive residues were obtained by the method of Petupessy et al. (E Pelupessy, S. Ravindranathan, G. Bodenhausen: J. Biomol. NMR 25, 265-280, 2003). The results suggest the presente of slow internal motions at 50 ~

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Principles and applications of cross-correlated relaxation in biomolecules

Cited by 67 publications

References 48 publications

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

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

Anisotropic Nuclear Spin Interactions for the Morphology Analysis of Proteins in Solution by NMR Spectroscopy

Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates

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