Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

3.2K
A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to...
3.2K
Non-conservative Forces01:17

Non-conservative Forces

10.1K
Non-conservative forces are dissipative forces such as friction or air resistance. These forces take energy away from a system as it progresses. Unlike conservative forces, non-conservative forces do not have potential energy associated with them. This is because the energy is lost to the system and cannot be turned into useful work later.
Also unlike their conservative counterparts, they are path-dependent; where the object starts and stops does matter. For example, a grinding wheel applies a...
10.1K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.8K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.8K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.3K
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
1.3K
Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

6.2K
The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
6.2K
Force and Potential Energy in One Dimension01:13

Force and Potential Energy in One Dimension

6.6K
Force can be calculated from the expression for potential energy, which is a function of position. The component of a conservative force, in a particular direction, equals the negative of the derivative of the corresponding potential energy with respect to the displacement in that direction. For regions where potential energy changes rapidly with displacement, the work done and force is maximum. Also, when force is applied along the positive coordinate axis, the potential energy decreases with...
6.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Surviving salt fluctuations: stress and recovery in Halobacterium salinarum, an extreme halophilic Archaeon.

Scientific reports·2020
Same author

Thermodynamics of lipid multi-lamellar vesicles in presence of sterols at high hydrostatic pressure.

Scientific reports·2017
Same author

Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.

Journal of the Royal Society, Interface·2015
Same author

[Surveillance and detection of unusual events in toxicovigilance: Review of relevant methods].

Revue d'epidemiologie et de sante publique·2015
Same author

The relationship between socioeconomic indices and potentially zoonotic pathogens carried by wild Norway rats: a survey in Rhône, France (2010-2012).

Epidemiology and infection·2014
Same author

Dynamics measured by neutron scattering correlates with the organization of bioenergetics complexes in natural membranes from hyperthermophile and mesophile bacteria.

The European physical journal. E, Soft matter·2013

Related Experiment Video

Updated: Mar 2, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

1.2K

Protein flexibility from the dynamical transition: a force constant analysis.

D J Bicout1, G Zaccai

  • 1INFM-Operative Group Grenoble CRG IN13, 38042 Grenoble Cedex 9, France. bicout@ill.fr

Biophysical Journal
|February 27, 2001
PubMed
Summary
This summary is machine-generated.

This study characterizes protein dynamics using elastic scans, revealing a key transition around 200 K. This transition relates protein flexibility to force constants and free energy barriers, offering insights into molecular resilience.

More Related Videos

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

5.9K
Flexural Rigidity Measurements of Biopolymers Using Gliding Assays
07:55

Flexural Rigidity Measurements of Biopolymers Using Gliding Assays

Published on: November 9, 2012

11.2K

Related Experiment Videos

Last Updated: Mar 2, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

1.2K
Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

5.9K
Flexural Rigidity Measurements of Biopolymers Using Gliding Assays
07:55

Flexural Rigidity Measurements of Biopolymers Using Gliding Assays

Published on: November 9, 2012

11.2K

Area of Science:

  • Biophysics
  • Materials Science
  • Neutron Scattering

Background:

  • Neutron scattering provides insights into atomic motion dynamics.
  • Biological macromolecules exhibit temperature-dependent dynamical behavior linked to function.
  • Proteins show a dynamical transition around 200 K, shifting between harmonic and nonharmonic regimes.

Purpose of the Study:

  • To analyze elastic scans in terms of force constants and free energy barriers.
  • To characterize the dynamical transition in proteins.
  • To explore relationships between protein dynamics, function, and activity.

Main Methods:

  • Analysis of scattered neutron incoherent elastic intensity.
  • Measurement of elastic scans (mean-square displacements) as a function of temperature.
  • Application of a novel analysis approach to elastic scan data.

Main Results:

  • Identified a dynamical transition in proteins at approximately 200 K.
  • Quantified increased protein flexibility beyond the transition.
  • Associated this flexibility with a free energy barrier (DeltaG ≈ RT) and effective force constants (0.1-3 N/m).

Conclusions:

  • The developed analysis method provides parameters for characterizing protein molecular resilience.
  • Insights into the relationship between protein dynamics, function, and activity were gained.
  • Understanding these parameters is crucial for exploring protein behavior.