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Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Related Experiment Video

Updated: Jan 9, 2026

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

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

Published on: September 17, 2017

A membrane perspective on peptide-membrane interactions: recent results from solid-state NMR.

Laila Zaatouf¹, Hugo Legras-Hemonnot¹, Dror E Warschawski¹

¹Chimie Physique et Chimie du Vivant, CPCV, CNRS UMR 8228, Sorbonne Université, École normale supérieure, PSL University, 75005 Paris, France.

Biomedical Journal

|December 10, 2025

Summary

Solid-state NMR now examines lipid-protein interactions from the lipid viewpoint, even in live bacteria. This method aids in understanding antimicrobial peptides for new therapeutic development.

Keywords:

Lipid-protein interaction bacteria in vivo NMR lipids membrane solid-state NMR

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Last Updated: Jan 9, 2026

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

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

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Published on: December 16, 2013

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

Solid-state NMR (ssNMR) is established for studying proteins, particularly membrane and fibrillar types.
Traditionally, ssNMR focused on isotopically labeled proteins to determine structures and binding sites.
Recent advances shift focus to the lipid perspective, examining lipid-protein interactions.

Purpose of the Study:

To highlight the growing importance of studying lipid-protein interactions from the lipid perspective.
To showcase the application of in vivo ssNMR in cellular contexts, specifically live bacteria.
To demonstrate the utility of various NMR isotopes (e.g., 2H, 31P, 13C, 15N, 1H, 19F) in these studies.

Main Methods:

Utilizing lipids and fatty acids (labeled or unlabeled) to study lipid-protein interactions.
Employing in vivo solid-state NMR (ssNMR) techniques on live bacteria.
Conducting NMR experiments on bacterial lipids and model membranes using multiple isotopes.

Main Results:

Demonstrated the feasibility of examining lipid-protein interactions from the lipid perspective in bacterial systems.
Showcased the application of various NMR isotopes for detailed molecular analysis.
Provided examples of ssNMR applied to bacterial membranes and model systems.

Conclusions:

The lipid-centric approach in ssNMR, especially in vivo, offers new insights into biological membranes.
This methodology is crucial for investigating the mechanisms of antimicrobial peptides.
Advances in ssNMR are vital for developing novel therapeutics targeting bacterial membranes.