Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

NMRhub: An NMR Data Ecosystem Spanning the Complete Data Lifecycle.

Journal of molecular biology·2026
Same author

Conformational Preferences for N-Glycans at the Surface of CEACAM1-Ig1.

ACS chemical biology·2025
Same author

Scalable cyberinfrastructure for experimental NMR data.

Scientific data·2025
Same author

AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2022
Same author

Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.

ACS chemical biology·2022
Same author

O-fucosylation stabilizes the TSR3 motif in thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond.

The Journal of biological chemistry·2022
Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026
Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026
Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026
Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026
Same journal

Retraction.

Science (New York, N.Y.)·2026
Same journal

Making time.

Science (New York, N.Y.)·2026
查看所有相关文章

相关实验视频

Updated: Jun 16, 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

仅使用骨干数据来确定较大的蛋白质的NMR结构.

Srivatsan Raman1, Oliver F Lange, Paolo Rossi

  • 1Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.

Science (New York, N.Y.)
|February 6, 2010
PubMed
概括
此摘要是机器生成的。

这项研究引入了一种使用核磁共振 (NMR) 数据来确定蛋白质结构的新方法. 它准确地模拟蛋白质结构,而不依赖于复杂的侧链赋值,简化了更大的蛋白质的过程.

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

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

相关实验视频

Last Updated: Jun 16, 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

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 生物物理学的生物物理.

背景情况:

  • 使用核磁共振 (NMR) 进行传统的蛋白质结构确定,主要依赖侧链质子对质子的距离.
  • 侧链共振的分配是传统的基于NMR的结构确定中的劳动密集和易出错的步骤.
  • 较大的蛋白质 (>15 kDa) 通常需要化来抑制核放松,增加了结构确定的复杂性.

研究的目的:

  • 开发和验证一种用于蛋白质结构确定的新方法,可以绕过广泛的侧链NMR数据的需求.
  • 为了能够在没有传统的侧链共振分配的情况下,准确地确定高达25千多的蛋白质结构.
  • 通过克服当前方法的局限性,促进对较大的蛋白质进行常规的NMR结构确定.

主要方法:

  • 将骨干化学转移,残余二极合和胺质子距离纳入罗塞塔蛋白质结构建模方法.
  • 使用稀疏的NMR数据来引导对蛋白质折叠景观中低能度构造的构造性搜索.
  • 利用罗塞塔全原子能量函数来定义计算的蛋白质模型的细节.

主要成果:

  • 在不依赖侧链NMR信息的情况下,确定了高达25千多的蛋白质的精确蛋白质结构.
  • 新方法有效地使用稀疏的NMR数据来指导构造性搜索,减少对劳动密集型任务的依赖.
  • 该方法与较大的蛋白质所需的化协议兼容,消除了一个重要的障碍.

结论:

  • 蛋白质结构的确定可以在没有广泛的侧链NMR赋值的情况下准确地实现,从而简化了该过程.
  • 骨干NMR数据和先进的计算建模的整合为结构生物学提供了一个强大的替代方案.
  • 这种方法显著提高了对更广泛的蛋白质大小的常规NMR结构确定的可行性,包括更大的和变质的蛋白质.