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Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...

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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Solid-state NMR ensemble dynamics as a mediator between experiment and simulation.

Taehoon Kim1, Sunhwan Jo, Wonpil Im

  • 1Department of Molecular Biosciences, Center for Bioinformatics, The University of Kansas, Lawrence, Kansas, USA.

Biophysical Journal
|June 22, 2011
PubMed
Summary
This summary is machine-generated.

Solid-state NMR (SSNMR) reveals transmembrane helix dynamics using multiple conformer models. This approach captures ensemble structures, providing accurate orientational and dynamic information missed by static models.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance

Background:

  • Solid-state NMR (SSNMR) is crucial for determining membrane protein orientations.
  • Deuterium quadrupolar splitting (DQS) analyzes transmembrane helix orientation using static models like GALA.
  • Static models may miss or misinterpret vital dynamic information of transmembrane helices.

Purpose of the Study:

  • To investigate the orientation and dynamics of WALP23 in a lipid bilayer using SSNMR.
  • To develop and apply multiple conformer models for SSNMR data analysis.
  • To compare SSNMR ensemble dynamics with static models and molecular dynamics simulations.

Main Methods:

  • Utilized deuterium ((2)H) quadrupolar splitting (DQS) in SSNMR.
  • Employed multiple conformer models with DQS restraint potential.
  • Determined an ensemble of structures for WALP23 in an implicit membrane.

Main Results:

  • A single conformer model yielded results similar to the GALA method (tilt angle 5.6 ± 3.2°).
  • Increasing conformers led to larger tilt angles (26.9 ± 6.7°), aligning with molecular dynamics simulations.
  • Ensemble structure distribution matched the 2D free energy surface of WALP23 orientation.

Conclusions:

  • SSNMR ensemble dynamics accurately extracts orientational and dynamic information from SSNMR observables.
  • This method reconciles discrepancies between molecular dynamics simulations and static model interpretations of DQS data.
  • Ensemble modeling provides a more comprehensive understanding of transmembrane helix behavior in membranes.