Publication

Predicting NMR relaxation rates in anisotropically tumbling proteins through networks of coupled rotators

Geoffrey Bodenhausen, Daniel Abergel
2008
Journal Articles

Abstract

We show that the prediction of N-15 relaxation rates in proteins can be extended to systems with anisotropic global, rotational diffusion by using a network of coupled rotators (NCR), starting from a three-dimensional structure. The relaxation rates predicted by this method are confronted in several examples with experiments performed by other groups. The NCR spectral density functions are compared with the results obtained from reduced spectral density mapping. The consequence of the timescales of internal motions on the predicted relaxation rates and the effects of the predicted local anisotropy-present only in the case of anisotropic overall tumbling-on dynamic parameters, are discussed.

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https://infoscience.epfl.ch/entities/publication/8303af21-8a77-4f6c-ad88-fd403946a50c

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Geoffrey Bodenhausen, Daniel Abergel
2008
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/8303af21-8a77-4f6c-ad88-fd403946a50c

About this result

Related concepts (20)

Nuclear Overhauser effect

The nuclear Overhauser effect (NOE) is the transfer of nuclear spin polarization from one population of spin-active nuclei (e.g. 1H, 13C, 15N etc.) to another via cross-relaxation. A phenomenological definition of the NOE in nuclear magnetic resonance spectroscopy (NMR) is the change in the integrated intensity (positive or negative) of one NMR resonance that occurs when another is saturated by irradiation with an RF field. The change in resonance intensity of a nucleus is a consequence of the nucleus being close in space to those directly affected by the RF perturbation.

Nuclear magnetic resonance

Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field (in the near field) and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca.

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Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

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