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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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IR spectra are divided into two main regions: the diagnostic region and the fingerprint region. The diagnostic region of the spectrum lies above 1500 cm−1. The absorptions resulting from single-bond vibrations of the N–H, C–H, and O–H stretch at higher wavenumbers and appear on the left side of the spectrum. The stretching absorptions of the C≡C and C≡N occur between 2100–2300 cm−1. In contrast, those arising from stretching absorptions of the...
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Updated: Feb 13, 2026

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

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Single-molecule peptide fingerprinting.

Jetty van Ginkel1,2, Mike Filius1,2, Malwina Szczepaniak1,2

  • 1Kavli Institute of Nanoscience, Delft University of Technology, 2629HZ Delft, The Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|March 14, 2018
PubMed
Summary
This summary is machine-generated.

This study introduces single-molecule Förster Resonance Energy Transfer (FRET)-based protein fingerprinting. This novel method uses a modified protease to analyze small protein samples, enabling low-abundance protein detection.

Keywords:
ClpXPpeptidesprotein analysissingle-molecule FRETsingle-molecule protein sequencing

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Area of Science:

  • Biochemistry and Molecular Biology
  • Analytical Chemistry
  • Proteomics

Background:

  • Proteomic analyses are crucial for understanding cellular pathways and organismal states.
  • Mass spectrometry is the standard for proteomic analysis but requires large sample quantities, limiting small-scale studies.
  • There is a need for sensitive techniques capable of analyzing limited protein samples.

Purpose of the Study:

  • To demonstrate a proof of concept for single-molecule Förster Resonance Energy Transfer (FRET)-based protein fingerprinting.
  • To develop a method for analyzing protein substrates using minimal sample amounts.
  • To explore the potential for detecting low-abundance proteins.

Main Methods:

  • Utilized the AAA+ protease ClpXP for scanning peptides.
  • Employed donor fluorophore-labeled ClpP to sequentially read FRET signals from acceptor-labeled amino acids within peptides.
  • Repurposed ClpXP for unidirectional processing with high processivity.

Main Results:

  • Successfully demonstrated single-molecule FRET-based protein fingerprinting.
  • The repurposed ClpXP system showed high processivity and unidirectional peptide scanning.
  • The technique has the potential to detect proteins present in low abundance.

Conclusions:

  • Single-molecule FRET-based protein fingerprinting is a viable approach for analyzing protein substrates.
  • The method is suitable for studies requiring small sample quantities.
  • This technique offers a promising alternative for protein sequencing and low-abundance protein detection.