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Related Concept Videos

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...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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...
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the others.
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...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

A new algorithm for reliable and general NMR resonance assignment.

Elena Schmidt1, Peter Güntert

  • 1Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt am Main, Germany.

Journal of the American Chemical Society
|July 17, 2012
PubMed
Summary
This summary is machine-generated.

The FLYA algorithm automates protein resonance assignment using NMR data, achieving high accuracy and outperforming existing methods for reliable structural studies.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Chemistry

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for determining protein structures.
  • Automated resonance assignment is essential for efficient and accurate structural analysis.
  • Existing assignment strategies can be limited by sequential data processing and error propagation.

Purpose of the Study:

  • To develop and validate the FLYA automated resonance assignment algorithm.
  • To assess the accuracy and reliability of FLYA compared to manual and existing automated methods.
  • To demonstrate FLYA's capability in handling diverse NMR experimental data for proteins.

Main Methods:

  • FLYA utilizes peak lists from multidimensional through-bond and through-space NMR experiments.
  • The algorithm integrates all experimental data simultaneously, optimizing redundancy.
  • It maps expected protein peaks to measured experimental peaks using defined transfer pathways.

Main Results:

  • FLYA achieved 96-99% accuracy for backbone and 90-91% for all assignable resonances.
  • Accuracy is robust against missing or artifact peaks and peak position errors.
  • FLYA produced significantly fewer erroneous assignments (40-142% less) than two other algorithms.

Conclusions:

  • FLYA offers a reliable and flexible alternative to manual and semi-automated NMR resonance assignment.
  • The algorithm's simultaneous data integration circumvents common assignment pitfalls.
  • FLYA enhances the efficiency and accuracy of NMR-based protein structure determination.