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関連する概念動画

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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Updated: Jun 26, 2026

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

13Cアルファ化学シフトテンソールを用いてタンパク質構造の精製.

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
まとめ

私たちは,タンパク質構造の決定のための新しい化学シフトテンザー (CST) 力場を開発しました. Xplor-NIHにCSTの拘束を組み込むことで,GB1タンパク質構造の精度と精度が向上しました.

科学分野:

  • バイオフィジックス 生物物理学
  • 構造生物学 構造生物学とは
  • コンピューティング・ケミストリー

背景:

  • 精密なタンパク質構造の決定は,生物学的機能を理解するために極めて重要です.
  • タンパク質の構造を精製するための既存の方法は,精度と正確性において限界があります.

研究 の 目的:

  • タンパク質構造の精錬のための新しい化学シフトテンソール (CST) 力場を開発および検証.
  • Xplor-NIHを使用してタンパク質構造の決定の精度と正確性に対するCST制限の影響を評価する.

主な方法:

  • タンパク質 GB1.1 の各アミノ酸に対する得られた (13) C アルファ化学シフトテンソール.
  • CST力場を開発し,Xplor-NIH構造決定プログラムに統合しました.
  • 比較されたGB1構造は,CSTの拘束装置とそれなしで,他の実験的拘束装置と並行して決定された.

主要な成果:

  • CSTの拘束装置で精製されたGB1の構造は,それ以外の構造と比較して精度が向上したことを示した.
  • CSTの制限を組み込むことで,より正確なタンパク質構造が得られました.
  • 他の拘束装置と組み合わせると,CSTは既存のX線構造の根の正方形の平均誤差を約1.0 Åに減らしました.

さらに関連する動画

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

関連する実験動画

Last Updated: Jun 26, 2026

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

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

結論:

  • 化学シフトテンソーは,精度と精度を高め,タンパク質構造の精錬に価値があります.
  • このアプローチにより,タンパク質構造の正確なデノボの決定が容易になります.
  • 開発されたCST力場と方法論は,構造生物学の研究に幅広い意味を持つ.