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Related Experiment Video

Updated: May 27, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
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Determining serpin conformational distributions with single molecule fluorescence.

Nicole Mushero1, Anne Gershenson

  • 1School of Medicine, University of Massachusetts, Worcester, Massachusetts, USA.

Methods in Enzymology
|November 15, 2011
PubMed
Summary

Single molecule fluorescence (SMF) reveals how serpin protein structures change, aiding understanding of polymerization and protease interactions. This technique helps differentiate functional and dysfunctional serpin forms.

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Last Updated: May 27, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

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Published on: May 30, 2021

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy
08:47

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy

Published on: January 25, 2020

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Area of Science:

  • Biochemistry and Biophysics
  • Molecular Biology
  • Protein Dynamics

Background:

  • Serpins exhibit conformational plasticity, leading to functional and dysfunctional states.
  • Understanding serpin conformational dynamics is crucial for their biological roles.
  • Existing methods struggle to resolve heterogeneous protein populations.

Purpose of the Study:

  • To elucidate conformational distributions of serpins using single molecule fluorescence (SMF).
  • To monitor dynamic changes in serpin conformations over time.
  • To characterize serpin polymerization and protease-serpin interactions.

Main Methods:

  • Application of single molecule fluorescence (SMF) techniques.
  • Utilizing fluorescence correlation spectroscopy (FCS) for polymerization studies.
  • Employing single pair Förster resonance energy transfer (spFRET) for protease-serpin complexes.

Main Results:

  • SMF effectively characterizes conformational distributions and dynamics.
  • FCS revealed a second lag phase in alpha-1-antitrypsin polymerization.
  • spFRET indicated protease-dependent structural disruption in serpin complexes.

Conclusions:

  • SMF is a powerful tool for studying serpin conformational heterogeneity.
  • These methods provide insights into serpin polymerization mechanisms.
  • Further development of SMF, combined with encapsulation, promises deeper understanding of serpin folding and interactions.