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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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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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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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Intermolecular Forces in Solutions02:28

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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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Force01:06

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Forces affect every moment of our life. Our bodies are held to the Earth by force, and they are held together by the forces of charged particles. When we open a door, walk down a street, lift a fork, or touch a baby's face, we are applying force. Our body's atoms are held together by electrical forces, and the core of an atom, called the nucleus, is held together by the strongest force known to us—nuclear force.
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The equilibrium of a two-force body is a particular case that is often encountered in practical applications. A two-force body is a rigid body that is subjected to only two external forces. For such a body to be in equilibrium, the two forces must have the same magnitude, the same line of action, and the opposite direction.
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Covalent Attachment of Single Molecules for AFM-based Force Spectroscopy
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Covalent Attachment of Single Molecules for AFM-based Force Spectroscopy

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High-Resolution AFM-Based Force Spectroscopy.

Krishna P Sigdel1, Anna E Pittman1, Tina R Matin1,2

  • 1Department of Physics and Astronomy, University of Missouri, Columbia, MO, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2018
PubMed
Summary
This summary is machine-generated.

This study presents two atomic force microscopy cantilever modification methods for precise biomolecular force measurements. These techniques enhance force precision across low and high frequencies, enabling detailed lipid-protein interaction studies.

Keywords:
Atomic force microscopyCantileverFIBFunctionalizationInteractionLipid bilayerPeptideTips

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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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Area of Science:

  • Biophysics
  • Materials Science
  • Nanotechnology

Background:

  • Atomic force microscopy (AFM)-based force spectroscopy is a key technique for probing molecular interactions.
  • Recent advancements have significantly improved the force and time resolution of AFM.
  • Cantilever modifications are crucial for achieving high-precision force measurements.

Purpose of the Study:

  • To detail two AFM cantilever modification procedures for high force precision.
  • To enable site-specific attachment of biomolecules for force spectroscopy.
  • To compare the performance of modified cantilevers in studying lipid-protein interactions.

Main Methods:

  • A straightforward method to remove metal coatings from commercial cantilevers for sub-pN force precision at low frequencies (<50 Hz).
  • A focused ion beam milling procedure for maintaining high force precision at enhanced temporal bandwidths.
  • Site-specific biomolecule attachment to the cantilever tip apex.

Main Results:

  • Demonstrated sub-pN force precision and stability at low frequencies using a simplified cantilever modification.
  • Achieved high force precision at enhanced bandwidths with focused ion beam milling.
  • Successfully applied both methods for site-specific biomolecule functionalization.

Conclusions:

  • Two distinct AFM cantilever modification techniques offer tailored solutions for precise force spectroscopy.
  • These methods enhance the study of biomolecular interactions, such as lipid-protein binding.
  • The choice of modification depends on the required force precision and temporal bandwidth.