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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...
Carbon-13 (¹³C) NMR: Overview01:10

Carbon-13 (¹³C) NMR: Overview

Carbon-13 is a naturally occurring NMR-active isotope of carbon with a low natural abundance of 1.1%. In contrast, carbon-12 is the most abundant isotope of carbon with zero nuclear spin. Therefore, it is NMR inactive. The gyromagnetic ratio of carbon-13 is smaller than that of protons. As a result, carbon-13 resonance is about 6000 times weaker than proton resonance. For a given magnetic field strength, the resonance frequency of carbon-13 is about one-fourth of the resonance frequency for...
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...
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
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 Of Amines01:19

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Refinamiento de la estructura proteica mediante el uso de tensores de desplazamiento químico 13C alfa.

Benjamin J Wylie1, Charles D Schwieters, Eric Oldfield

  • 1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.

Journal of the American Chemical Society
|January 7, 2009
PubMed
Resumen

Desarrollamos un nuevo campo de fuerza de tensor de desplazamiento químico (CST) para la determinación de la estructura de las proteínas. La incorporación de restricciones CST en Xplor-NIH mejoró la exactitud y precisión de las estructuras de proteínas GB1.

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Área de la Ciencia:

  • La biofísica es la biofísica.
  • Biología Estructural Biología estructural.
  • Química computacional es la química computacional.

Sus antecedentes:

  • La determinación precisa de la estructura de las proteínas es crucial para comprender la función biológica.
  • Los métodos existentes para el refinamiento de la estructura de las proteínas tienen limitaciones en cuanto a precisión y exactitud.

Objetivo del estudio:

  • Desarrollar y validar un nuevo campo de fuerza de tensor de desplazamiento químico (CST) para el refinamiento de la estructura de las proteínas.
  • Evaluar el impacto de las restricciones de CST en la precisión y exactitud de la determinación de la estructura de las proteínas utilizando Xplor-NIH.

Principales métodos:

  • Obtenidos (13) C tensores de desplazamiento químico alfa para cada aminoácido en la proteína GB1.1.
  • Desarrolló un campo de fuerza CST y lo integró en el programa de determinación de estructura Xplor-NIH.
  • Comparación de estructuras GB1 determinadas con y sin restricciones CST, junto con otras restricciones experimentales.

Principales resultados:

  • Las estructuras GB1 refinadas con restricciones CST demostraron una precisión mejorada en comparación con las sin.
  • La inclusión de restricciones de CST condujo a estructuras de proteínas más precisas.
  • En combinación con otras restricciones, los CST redujeron el error cuadrado de la raíz media de las estructuras de rayos X existentes a aproximadamente 1,0 Å.

Conclusiones:

  • Los tensores de desplazamiento químico son valiosos para el refinamiento de la estructura de las proteínas, mejorando tanto la precisión como la precisión.
  • Este enfoque facilita la determinación precisa de la estructura de las proteínas de novo.
  • El campo de fuerza y la metodología CST desarrollados tienen amplias implicaciones para la investigación en biología estructural.