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

Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

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.
EDTA: Conditional Formation Constant01:09

EDTA: Conditional Formation Constant

Each EDTA molecule has six binding sites: four carboxyl groups and two amino groups. The fully protonated form of EDTA is represented as H6Y2+. However, it can exist in different forms, H5Y+, H4Y, H3Y−, H2Y2−, and HY3−, depending on the pH of the solution. In very basic solutions with pH > 10.17, the fully deprotonated form, Y4−, is the predominant species that readily complexes with metal ions in a 1:1 ratio.
For the equilibrium reaction of the metal with the Y4− form of EDTA, the formation...

You might also read

Related Articles

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

Sort by
Same author

PEERing into the Future: Benchmarking the ANSTO Australian Synchrotron's Very-High-Energy Electron Linac for Ultra-High Dose-Rate, In Vivo FLASH Radiotherapy Research.

Cancers·2026
Same author

A fasting-mimicking environment enhances procaspase-activating compound 1 in 2D and 3D glioma cell models.

Cell cycle (Georgetown, Tex.)·2026
Same author

Ornithine lipids from <i>Akkermansia muciniphila</i> are dynamically modulated in colitis and shape macrophage inflammatory responses.

Gut microbes·2025
Same author

Self-assembled cell-scale containers made from DNA origami membranes.

Nature materials·2025
Same author

Point cloud dosimetry framework for preclinical microbeam radiation therapy.

Physica medica : PM : an international journal devoted to the applications of physics to medicine and biology : official journal of the Italian Association of Biomedical Physics (AIFB)·2025
Same author

Hierarchical Structural Organization in Bioinspired Peptide Coacervate Microdroplets.

ACS nano·2025
Same journal

Disruption of bacterial membranes by plant extracts of celandine and dandelion: microbiological and langmuir monolayer studies.

European biophysics journal : EBJ·2026
Same journal

Challenging cases for AlphaFold: two multidomain proteins with zinc-binding-, phosphorylation- or dimerization-driven conformational changes.

European biophysics journal : EBJ·2026
Same journal

In sample pH measurement by <sup>31</sup>P phosphate NMR: application to measure the intrinsic GTPase activity of Rab1a.

European biophysics journal : EBJ·2026
Same journal

The MOlecular-Scale Biophysics Research Infrastructure (MOSBRI) Project and its Outcomes.

European biophysics journal : EBJ·2026
Same journal

Bitter taste TAS2R14 and TAS2R46 receptors bound to G proteins: comparison of cryo-EM, AlphaFold, and molecular dynamics structures.

European biophysics journal : EBJ·2026
Same journal

Homologous series of N-acylmelatonins: synthesis, biophysical studies, enhanced antioxidant, antimicrobial and anticancer activities.

European biophysics journal : EBJ·2026
See all related articles

Related Experiment Video

Updated: Jul 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Solvent isotope effect on macromolecular dynamics in E. coli.

Marion Jasnin1, Moeava Tehei, Martine Moulin

  • 1Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 41 rue Jules Horowitz, 38027 Grenoble, France. jasnin@ill.fr

European Biophysics Journal : EBJ
|February 21, 2008
PubMed
Summary
This summary is machine-generated.

Solvent isotope effects impact macromolecular dynamics in E. coli. Deuterium oxide (D2O) reduces flexibility and resilience compared to water (H2O), influencing cellular structure and function.

More Related Videos

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Related Experiment Videos

Last Updated: Jul 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

  • Biophysics
  • Structural Biology
  • Cellular Dynamics

Background:

  • Macromolecular dynamics are crucial for cellular function.
  • Solvent properties, like isotopic composition, can influence these dynamics.
  • Understanding these effects in vivo is essential for comprehending cellular behavior.

Purpose of the Study:

  • To investigate the effects of water (H2O) versus deuterium oxide (D2O) on the average dynamics of macromolecules within living E. coli bacteria.
  • To quantify changes in macromolecular flexibility and structural resilience under different solvent conditions.

Main Methods:

  • Elastic incoherent neutron scattering (EINS) was employed to probe atomic fluctuations.
  • Measurements were conducted on living E. coli in H2O and D2O near physiological temperatures.
  • Analysis focused on mean square fluctuation (MSF) and effective force constants ([Symbol: see text]k'[Symbol: see text]) to assess dynamics and resilience.

Main Results:

  • Macromolecular flexibility (MSF) was significantly lower in D2O compared to H2O.
  • Structural resilience ([Symbol: see text]k'[Symbol: see text]) was also reduced in D2O.
  • These changes are attributed to differences in hydrophobic effects and entropy between H2O and D2O.

Conclusions:

  • Deuterium oxide alters the average dynamics of macromolecules in living cells.
  • The stronger hydrophobic effect in D2O likely leads to more compact structures with reduced flexibility.
  • Increased conformational entropy in D2O may contribute to the observed changes in resilience.