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Related Concept Videos

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Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen...
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The formation of a solution is an example of a spontaneous process, a process that occurs under specified conditions without energy from some external source.
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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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Electricity is generated by either electrons or ions flowing through a solution or a conducting medium. This flow of electrons or specifically electrical charge is defined as an electric current. When electrons move through a wire, they generate an electric current. It can be recalled  that in a redox reaction, electrons are lost and gained. In the spontaneous redox reaction of zinc  with copper, when zinc is immersed in a copper ion solution, a transfer of electrons from one substance to...
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Covalent Attachment of Single Molecules for AFM-based Force Spectroscopy
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AFM-Based Single-Molecule Force Spectroscopy of Proteins.

Zackary N Scholl1, Piotr E Marszalek2

  • 1Department of Physics, University of Alberta, Edmonton, AB, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2018
PubMed
Summary

Single-molecule force spectroscopy (SMFS) using atomic force microscopy (AFM) offers precise insights into protein mechanics. This review details AFM-SMFS methods for studying protein folding, interactions, and misfolding.

Keywords:
Atomic force spectroscopyProtein foldingProtein mechanicsProtein misfoldingSingle molecule

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Single-molecule force spectroscopy by atomic force microscopy (AFM-SMFS) has revolutionized the study of molecular mechanics.
  • Over two decades, AFM-SMFS has yielded critical data on the mechanical properties and force-induced rearrangements of biomolecules like DNA and proteins.

Purpose of the Study:

  • This chapter focuses on the application of AFM-SMFS specifically to protein research.
  • It aims to elucidate protein folding pathways, kinetics, interactions, and misfolding mechanisms.

Main Methods:

  • Detailed experimental procedures for conducting SMFS-AFM experiments are described.
  • Key steps include meticulous purification of protein samples.
  • Proper setup and calibration of AFM instrumentation are emphasized.

Main Results:

  • AFM-SMFS provides abundant information on protein folding dynamics.
  • The technique is instrumental in understanding protein interactions and misfolding.
  • It allows for sensitive investigation and manipulation of single-molecule mechanical properties.

Conclusions:

  • AFM-SMFS is a powerful tool for dissecting complex protein behaviors at the single-molecule level.
  • The chapter provides a guide for researchers to perform and analyze SMFS-AFM experiments.
  • This methodology enhances our understanding of protein structure-function relationships.