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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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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...
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Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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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.
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
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Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

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

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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...
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Related Experiment Video

Updated: Mar 9, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
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(S)Pinning down protein interactions by NMR.

Kaare Teilum1, Micha Ben Achim Kunze1, Simon Erlendsson1

  • 1Structural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200, Copenhagen N, Denmark.

Protein Science : a Publication of the Protein Society
|December 27, 2016
PubMed
Summary

Nuclear Magnetic Resonance (NMR) spectroscopy is a versatile technique for studying protein interactions. This review guides non-specialists on using NMR to quantitatively analyze protein-ligand binding, covering methods and potential challenges.

Keywords:
affinitybindingchemical shiftdissociation constantexchangeligandspectroscopy

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Area of Science:

  • Biochemistry and Molecular Biology
  • Spectroscopy
  • Structural Biology

Background:

  • Protein molecules act as diverse communication platforms, interacting with various molecules from small compounds to macromolecules.
  • Quantitative analysis of protein interactions is crucial for understanding molecular communication, encompassing reaction rates, thermodynamics, and constituent proportions.
  • No single method can fully capture all protein reaction types due to wide variations in affinities, rates, and state lifetimes.

Purpose of the Study:

  • To provide an accessible overview of Nuclear Magnetic Resonance (NMR) spectroscopy for non-specialists.
  • To explain how and when solution-state NMR is the preferred method for analyzing protein-ligand interactions.
  • To illustrate strategies for measuring binding constants and discuss potential challenges and improvements in NMR analyses.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy is presented as a versatile technique for quantitative and qualitative descriptions of protein interactions.
  • The review briefly covers theoretical background relevant to NMR spectroscopy.
  • Strategies for measuring binding constants in protein-ligand interactions using NMR are illustrated.

Main Results:

  • Solution NMR spectroscopy offers a comprehensive set of methods applicable to diverse protein interaction studies.
  • The review details practical approaches for utilizing NMR to quantify protein-ligand binding.
  • Examples of common pitfalls and optimization strategies for NMR-based interaction analysis are provided.

Conclusions:

  • Solution NMR spectroscopy is a powerful and versatile tool for the quantitative analysis of protein interactions, particularly protein-ligand binding.
  • This review serves as a guide for researchers to effectively employ NMR spectroscopy in their studies.
  • Understanding the method's limitations and employing appropriate strategies can enhance the accuracy and success of NMR analyses.