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

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.7K
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
3.7K
Proteomics01:33

Proteomics

7.3K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.3K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

8.7K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
8.7K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.7K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.3K
2.3K

You might also read

Related Articles

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

Sort by
Same author

Raman Evidence of Moiré Diamondene Formation by High-Pressure.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Synergistically Enhancing Light Harvesting and Mechanical Flexibility for Ultra-Flexible Organic Biosensors.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

Feed-Draw Printing Enables Monolithically Integrated Flexible Sensors With High Interfacial Toughness and Wide Linear Range.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

GhTTLL12 Coordinates With Transcriptional Regulators GhMML3 and GhMYB86 to Orchestrate Cotton Fibre Development Through Modulating Microtubule Dynamics.

Plant biotechnology journal·2026
Same author

The multichromosomal structure evolution of <i>Dendrobium</i> mitogenomes and new insights into interrelationships of recently radiated tribes in Epidendroideae (Orchidaceae).

Frontiers in plant science·2026
Same author

Semi-rational design of a hyperstable β-glucosidase Bgl1269 for enhanced soy Isoflavone bioconversion.

Food chemistry·2026

Related Experiment Video

Updated: Jun 28, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

1.9K

Protein Allostery Study in Cells Using NMR Spectroscopy.

Xiaoxu Chen1,2,3, Xueying Zhang1,2,3,4, Mingming Qin1,2,3

  • 1Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China.

Analytical Chemistry
|April 23, 2024
PubMed
Summary

Protein allostery differs in cells versus in vitro. Cellular environments create new allosteric pathways by altering protein interactions, impacting protein allostery significantly.

More Related Videos

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
10:25

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

Published on: March 9, 2021

3.3K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.2K

Related Experiment Videos

Last Updated: Jun 28, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

1.9K
Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
10:25

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

Published on: March 9, 2021

3.3K
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Protein allostery is well-documented in vitro but its behavior within the complex cellular environment remains largely unknown.
  • Understanding in-cell protein allostery is crucial for deciphering complex biological regulation and developing targeted therapeutics.

Purpose of the Study:

  • To investigate how protein allostery manifests and is modulated within a cellular environment compared to in vitro conditions.
  • To identify the factors contributing to altered allosteric behavior in cells.

Main Methods:

  • Development of a protein monomer-dimer equilibrium system to study allosteric effects.
  • Utilized Nuclear Magnetic Resonance (NMR) spectroscopy and a novel chemical shift linear fitting method to quantify binding dissociation constants.
  • Systematically analyzed 28 allosteric mutations, categorizing them as negative allosteric, nonallosteric, or positive allosteric modulators.

Main Results:

  • Approximately 50% of studied mutations exhibited altered allosteric states when transitioning from buffered solutions to cellular conditions.
  • Notably, several mutations identified as non-allosteric in vitro demonstrated positive allosteric modulation within cells.
  • Changes in protein allostery were directly correlated with interactions between the protein and the cellular milieu.

Conclusions:

  • The cellular environment profoundly influences protein allostery, creating distinct regulatory pathways not observed in vitro.
  • Interactions with cellular macromolecules transiently bind to protein sites, differentially altering free energies and generating novel allosteric effects.
  • This study reveals a new paradigm of protein allostery mediated by the cellular environment.