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Related Concept Videos

Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
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...

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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

Automated structure determination from NMR spectra.

Peter Güntert1

  • 1Institute of Biophysical Chemistry, Goethe-University Frankfurt am Main, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany. guentert@em.uni-frankfurt.de

European Biophysics Journal : EBJ
|September 23, 2008
PubMed
Summary

Automated Nuclear Magnetic Resonance (NMR) methods are revolutionizing protein structure determination. The FLYA algorithm offers fully automated analysis, overcoming previous efficiency limitations in structural biology.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for determining protein structures.
  • Manual analysis of NMR spectra is a time-consuming bottleneck in protein structure determination.
  • Automated methods are increasingly adopted for efficiency and accuracy.

Purpose of the Study:

  • To review current automated techniques for protein structure analysis using NMR.
  • To introduce the FLYA algorithm for fully automated NMR structure determination.
  • To highlight the potential of automation to overcome efficiency limitations in NMR-based structural biology.

Main Methods:

  • Overview of Nuclear Overhauser Effect (NOE)-based automated approaches.
  • Inclusion of methods utilizing residual dipolar couplings (RDCs) and chemical shifts.
  • Presentation of the FLYA algorithm for comprehensive automated structure calculation.

Main Results:

  • Automated assignment of distance restraints and calculation of 3D protein structures are now standard.
  • The FLYA algorithm enables complete automation, replacing manual spectral analysis.
  • Automation significantly enhances the efficiency of protein structure determination by NMR.

Conclusions:

  • Automated NMR methods are crucial for advancing structural biology.
  • The FLYA algorithm represents a significant step towards fully automated protein structure determination.
  • Overcoming manual analysis limitations will accelerate insights into protein function and mechanisms.