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Related Concept Videos

NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
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...
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
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.
Raman Spectroscopy Instrumentation: Overview01:26

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A conventional Raman spectrophotometer includes a laser source, a sample holding system, a wavelength selector, and a detector.
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Published on: September 17, 2017

A software framework for analysing solid-state MAS NMR data.

Tim J Stevens1, Rasmus H Fogh, Wayne Boucher

  • 1Department of Biochemistry, University of Cambridge, UK.

Journal of Biomolecular NMR
|September 29, 2011
PubMed
Summary
This summary is machine-generated.

New software features enhance solid-state magic-angle-spinning (MAS) NMR data analysis for proteins. These updates address limitations in current tools, improving protein structure and dynamics studies using solid-state NMR spectroscopy.

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Published on: November 2, 2018

Area of Science:

  • Biochemistry and Structural Biology
  • Analytical Chemistry
  • Spectroscopy

Background:

  • Solid-state magic-angle-spinning (MAS) NMR spectroscopy is crucial for studying protein structure, function, and dynamics.
  • Existing software tools for NMR data analysis are primarily designed for solution-state NMR and do not adequately address solid-state specific challenges.
  • This gap hinders the full potential of advanced solid-state MAS NMR methodologies.

Purpose of the Study:

  • To enhance the CcpNmr Analysis software package with features tailored for solid-state MAS NMR data.
  • To improve the analysis of complex solid-state NMR spectra, including spinning side bands and double quantum spectra.
  • To provide a robust platform for solid-state MAS NMR data management and programming.

Main Methods:

  • Development of new functionalities within the CcpNmr Analysis software.
  • Updates to the CCPN data model and experiment descriptions to incorporate solid-state NMR specific parameters and nomenclature.
  • Implementation of experiment prototypes for common solid-state MAS protein NMR experiments.

Main Results:

  • Introduction of features for easier identification of spinning side bands in solid-state NMR spectra.
  • Enabled straightforward analysis of double quantum spectra.
  • Automatic consideration of non-uniform labeling schemes and extensions to existing features for solid-state MAS data.

Conclusions:

  • The updated CcpNmr Analysis software significantly improves the analysis of solid-state MAS NMR data for proteins.
  • These advancements facilitate more detailed studies of protein structure, function, and dynamics.
  • The enhanced software serves as a valuable platform for data processing, programming, and archival in solid-state MAS NMR research.