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相关概念视频

Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the others.
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...
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...

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相关实验视频

Updated: May 20, 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

一种新的算法可用于可靠和一般的NMR共振赋值.

Elena Schmidt1, Peter Güntert

  • 1Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt am Main, Germany.

Journal of the American Chemical Society
|July 17, 2012
PubMed
概括

该FLYA算法使用NMR数据自动化蛋白质共振分配,实现高精度和超越可靠结构研究的现有方法.

科学领域:

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

背景情况:

  • 核磁共振 (NMR) 光谱对于确定蛋白质结构至关重要.
  • 自动共振分配对于高效准确的结构分析至关重要.
  • 现有的分配策略可以通过顺序数据处理和错误传播来限制.

研究的目的:

  • 开发和验证FLYA自动共振分配算法.
  • 与手动和现有的自动化方法相比,评估FLYA的准确性和可靠性.
  • 为了证明FLYA在处理各种蛋白质NMR实验数据方面的能力.

主要方法:

  • FLYA使用来自多维透过键和透过空间的NMR实验的峰值列表.
  • 该算法同时集成所有实验数据,优化冗余性.
  • 它将预期的蛋白质峰值映射到测量的实验峰值,使用定义的传输路径.

主要成果:

  • 对于骨干,FLYA的准确度达到96-99%,对于所有可指定的共振,准确度达到90-91%.
  • 准确性强大,可以抵御缺失或文物峰值和峰值位置错误.
  • 与其他两个算法相比,FLYA的错误分配数量显著减少 (40-142%) .

更多相关视频

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

The Identification of Sea Lamprey Pheromones Using Bioassay-Guided Fractionation
09:35

The Identification of Sea Lamprey Pheromones Using Bioassay-Guided Fractionation

Published on: July 17, 2018

相关实验视频

Last Updated: May 20, 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

The Identification of Sea Lamprey Pheromones Using Bioassay-Guided Fractionation
09:35

The Identification of Sea Lamprey Pheromones Using Bioassay-Guided Fractionation

Published on: July 17, 2018

结论:

  • FLYA提供了一种可靠和灵活的替代手动和半自动NMR共振分配.
  • 算法的同时数据集成绕过了常见的分配陷.
  • FLYA提高了基于NMR的蛋白质结构确定效率和准确性.