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Related Concept Videos

NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

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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...
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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.
The monochromatic laser source, typically using visible or near-infrared radiation, generates a highly focused beam of light. This light interacts with the molecules of the sample, scattering some of the light. Liquid and gaseous samples are usually tested in ordinary glass capillaries, while solids can be analyzed as powders packed in capillaries or as potassium...
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¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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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...
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Raman Spectroscopy: Overview01:20

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The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
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2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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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.
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2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

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Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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Automated projection spectroscopy in solid-state NMR.

Alexander Klein1,2, Suresh K Vasa1,2, Rasmus Linser3,4,5

  • 1Department of Chemistry, Ludwig-Maximilians-University Munich, Butenandtstr. 5-13, 81377, Munich, Germany.

Journal of Biomolecular NMR
|November 16, 2018
PubMed
Summary
This summary is machine-generated.

Higher-dimensionality solid-state NMR methods are crucial for assigning complex protein structures. Automated projection spectroscopy is demonstrated for micro-crystalline proteins, enhancing chemical shift assignments.

Keywords:
Data acquisitionMicro-crystalline proteinProjection spectroscopyProton detectionSolid-state NMR

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR is increasingly applied to large and complex protein samples.
  • Higher-dimensionality NMR techniques are becoming essential for accurate chemical shift assignments.
  • Solid-state NMR spectra show increasing similarity to solution NMR, enabling adaptation of advanced strategies.

Purpose of the Study:

  • To demonstrate the application of automated projection spectroscopy for solid-state NMR.
  • To address the need for improved methods in analyzing micro-crystalline protein structures.

Main Methods:

  • Application of automated projection spectroscopy.
  • Analysis of a micro-crystalline protein sample in the solid state.

Main Results:

  • Successful demonstration of automated projection spectroscopy on a micro-crystalline protein.
  • Validation of the technique for enhancing chemical shift assignments in solid-state NMR.

Conclusions:

  • Automated projection spectroscopy is a viable and powerful method for solid-state NMR analysis.
  • This technique facilitates unambiguous chemical shift assignments for complex protein systems.