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Related Concept Videos

Intermolecular Forces03:13

Intermolecular Forces

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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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Intermolecular forces (IMF) are electrostatic attractions arising from charge-charge interactions between molecules. The strength of the intermolecular force is influenced by the distance of separation between molecules. The forces significantly affect the interactions in solids and liquids, where the molecules are close together. In gases, IMFs become important only under high-pressure conditions (due to the proximity of gas molecules). Intermolecular forces dictate the physical properties of...
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Atomic Force Microscopy01:08

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Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
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Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, and solubilities (miscibilities) of substances. Molar mass, molecular shape, and polarity affect the strength of different intermolecular forces, which influence the magnitude of physical properties across a family of molecules.
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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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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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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope.

Zackary N Scholl1, Qing Li1, Eric Josephs1

  • 1Mechanical Engineering and Materials Science, Duke University.

Journal of Visualized Experiments : Jove
|March 19, 2019
PubMed
Summary

This study provides a detailed protocol for Atomic Force Microscopy-based Single-Molecule Force Spectroscopy (AFM-SMFS) experiments. It guides researchers in measuring protein unfolding and refolding, overcoming challenges in this advanced biophysical technique.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Protein folding from amino acid sequence to 3D structure is a key biological problem.
  • Atomic Force Microscopy (AFM) enables single-molecule stretching to study protein dynamics.
  • AFM-based Single-Molecule Force Spectroscopy (AFM-SMFS) measures high-energy protein conformations inaccessible by bulk methods.

Purpose of the Study:

  • To provide a comprehensive protocol for conducting AFM-SMFS experiments.
  • To guide researchers in achieving reliable results in single-molecule force spectroscopy.
  • To detail procedures and data analysis for protein unfolding and refolding studies.

Main Methods:

  • Detailed illustration of Atomic Force Microscopy (AFM) principles.
  • Extensive protocols and procedures for AFM-SMFS experiments.
  • Guidance on data analysis for mechanical unfolding measurements.

Main Results:

  • Demonstration of representative AFM-SMFS results for single protein mechanical unfolding.
  • Provision of troubleshooting strategies for common experimental issues.
  • Establishment of a guideline for successful SMFS experiments.

Conclusions:

  • AFM-SMFS is a powerful technique for investigating protein folding and mechanical properties.
  • A detailed protocol is crucial for the successful implementation of AFM-SMFS.
  • This study facilitates broader application of AFM-SMFS in biophysical research.