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

Protein Denaturation01:28

Protein Denaturation

9.7K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
9.7K
Free Energy Changes for Nonstandard States03:25

Free Energy Changes for Nonstandard States

13.6K
The free energy change for a process taking place with reactants and products present under nonstandard conditions (pressures other than 1 bar; concentrations other than 1 M) is related to the standard free energy change according to this equation:
13.6K
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

2.7K
The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For...
2.7K
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

9.1K
Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
9.1K
ATP Synthase: Structure01:18

ATP Synthase: Structure

15.9K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
15.9K

You might also read

Related Articles

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

Sort by
Same author

Disordered N-Terminal Tail "Wags the Dog" in Human Thymidylate Synthase.

Biochemistry·2026
Same author

The Power of Protein Dynamics in Binding and Allostery.

Biochemistry·2026
Same author

A flexible, allosteric loop regulates protein activity and rewires electrostatics.

Protein science : a publication of the Protein Society·2025
Same author

Classification of Samples via Neural-Network Augmented Two-Dimensional Infrared Spectroscopy.

The journal of physical chemistry. B·2025
Same author

Mixed, nonclassical behavior in a classic allosteric protein.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Increasing Pump-Probe Signal toward Asymptotic Limits.

The journal of physical chemistry. B·2023

Related Experiment Video

Updated: Feb 19, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.5K

Protein Mass Effects on Formate Dehydrogenase.

Chethya Ranasinghe1, Qi Guo1, Paul J Sapienza2

  • 1Department of Chemistry, University of Iowa , Iowa City, Iowa 52242-1727, United States.

Journal of the American Chemical Society
|October 31, 2017
PubMed
Summary

Heavy enzyme studies reveal that protein mass affects both fast vibrations and slower electrostatic dynamics during catalysis. This research explores the interplay between protein motion and enzymatic reactions, offering new insights into enzyme mechanisms.

More Related Videos

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.5K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Related Experiment Videos

Last Updated: Feb 19, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

10.5K
Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.5K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Area of Science:

  • Biochemistry
  • Enzyme kinetics
  • Protein dynamics

Background:

  • Isotopically labeled enzymes (heavy enzymes) are used to probe the role of protein dynamics in catalysis.
  • The hypothesis is that increased protein mass alters vibrational frequencies without changing electrostatics.
  • Previous studies on heavy enzymes have yielded ambiguous results regarding their impact on catalysis.

Purpose of the Study:

  • To investigate the temperature-dependence of kinetic isotope effects in formate dehydrogenase using heavy enzymes.
  • To examine how protein mass influences the distribution of H-donor to H-acceptor distances during catalysis.
  • To differentiate between Born-Oppenheimer (vibrational) and non-Born-Oppenheimer (electrostatic) effects in enzyme catalysis.

Main Methods:

  • Utilized temperature-dependence of intrinsic kinetic isotope effects.
  • Employed steady-state and single-turnover measurements.
  • Analyzed protein mass dependence of donor-acceptor distance and forward commitment to catalysis.

Main Results:

  • Heavy enzyme dynamics were altered, diminishing motions critical for transition state sampling.
  • Findings suggest contributions from both fast, vibrational (Born-Oppenheimer) and slower, electrostatic (non-Born-Oppenheimer) processes.
  • Protein mass modulation impacted local vibrations and macromolecular electrostatics.

Conclusions:

  • Both Born-Oppenheimer and non-Born-Oppenheimer effects are observed in heavy enzyme studies.
  • Isotopic labeling can have system-specific effects on enzyme dynamics.
  • Heavy enzyme studies are a valuable technique for investigating the link between protein dynamics and catalysis.