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相关概念视频

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
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

使用13Cα化学转移张量器精制蛋白质结构.

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
概括

我们开发了一种新的化学转移张量 (CST) 力场,用于蛋白质结构的确定. 在Xplor-NIH中加入CST束可以提高GB1蛋白结构的准确性和精度.

科学领域:

  • 生物物理学的生物物理.
  • 结构生物学 结构生物学
  • 计算化学计算化学

背景情况:

  • 准确的蛋白质结构确定对于理解生物功能至关重要.
  • 目前用于精制蛋白质结构的现有方法在精度和准确性方面存在局限.

研究的目的:

  • 开发和验证一种新的化学转移张量 (CST) 力场,用于精制蛋白质结构.
  • 评估CST限制对使用Xplor-NIH的蛋白质结构确定精度和准确性的影响.

主要方法:

  • 获得的 (13)Cα化学转移张量为蛋白质GB1.1中的每个氨基酸.
  • 开发了一个CST力场,并将其集成到Xplor-NIH结构确定程序中.
  • 与其他实验性约束装置一起,与CST约束装置一起和没有CST约束装置一起确定的比较GB1结构.

主要成果:

  • 与没有CST束器的结构相比,用CST束器精制的GB1结构显示出更高的精度.
  • 包括CST限制因素导致了更准确的蛋白质结构.
  • 结合其他约束,CSTs将现有X射线结构的根-平均平方误差降低到大约1.0 Å.

结论:

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

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

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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

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

  • 化学转移张量器对于蛋白质结构的精细化是有价值的,提高了准确性和精度.
  • 这种方法有助于准确的新蛋白质结构的确定.
  • 开发的CST力场和方法对结构生物学研究有广泛的影响.