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Related Concept Videos

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...

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Related Experiment Video

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

NMR structure determination for larger proteins using backbone-only data.

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
Summary
This summary is machine-generated.

This study introduces a new method for protein structure determination using nuclear magnetic resonance (NMR) data. It accurately models protein structures without relying on complex side-chain assignments, simplifying the process for larger proteins.

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

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Conventional protein structure determination using nuclear magnetic resonance (NMR) heavily relies on side-chain proton-to-proton distances.
  • The assignment of side-chain resonances is a labor-intensive and error-prone step in traditional NMR-based structure determination.
  • Larger proteins (>15 kDa) often require deuteration to suppress nuclear relaxation, adding complexity to structure determination.

Purpose of the Study:

  • To develop and validate a novel methodology for protein structure determination that bypasses the need for extensive side-chain NMR data.
  • To enable accurate structure determination for proteins up to 25 kilodaltons without traditional side-chain resonance assignments.
  • To facilitate routine NMR structure determination for larger proteins by overcoming limitations of current methods.

Main Methods:

  • Incorporation of backbone chemical shifts, residual dipolar couplings, and amide proton distances into the Rosetta protein structure modeling methodology.
  • Utilizing sparse NMR data to guide conformational search towards low-energy conformations within the protein folding landscape.
  • Leveraging the Rosetta all-atom energy function to define the details of the computed protein models.

Main Results:

  • Accurate protein structures were determined for proteins up to 25 kilodaltons without relying on side-chain NMR information.
  • The new method effectively uses sparse NMR data to guide the conformational search, reducing reliance on labor-intensive assignments.
  • The methodology is compatible with deuteration protocols necessary for larger proteins, removing a significant hurdle.

Conclusions:

  • Protein structure determination can be achieved accurately without extensive side-chain NMR assignments, simplifying the process.
  • The integration of backbone NMR data and advanced computational modeling offers a powerful alternative for structural biology.
  • This approach significantly enhances the feasibility of routine NMR structure determination for a broader range of protein sizes, including larger and deuterated proteins.