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 Folding01:25

Protein Folding

8.4K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.4K
Protein and Protein Structure02:15

Protein and Protein Structure

80.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
80.4K
Protein Organization01:24

Protein Organization

6.8K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.8K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.9K
Sulfur Assimilation01:20

Sulfur Assimilation

64
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
64
Amino Acid Catabolism01:18

Amino Acid Catabolism

124
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
124

You might also read

Related Articles

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

Sort by
Same author

A structure-based tool to interpret the significance of kinase mutations in clinical next generation sequencing in cancer.

Frontiers in oncology·2025
Same author

A role for pH dynamics regulating transcription factor DNA-binding selectivity.

Nucleic acids research·2025
Same author

Identifying FUS amyotrophic lateral sclerosis disease signatures in patient dermal fibroblasts.

Developmental cell·2024
Same author

A role for pH dynamics regulating transcription factor DNA binding selectivity.

bioRxiv : the preprint server for biology·2024
Same author

BCR::ABL1 kinase N-lobe mutants confer moderate to high degrees of resistance to asciminib.

Blood·2024
Same author

Integration of Genomic Sequencing Drives Therapeutic Targeting of PDGFRA in T-Cell Acute Lymphoblastic Leukemia/Lymphoblastic Lymphoma.

Clinical cancer research : an official journal of the American Association for Cancer Research·2023

Related Experiment Video

Updated: Aug 27, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

1.8K

Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.

Diego Garrido Ruiz1, Angelica Sandoval-Perez1, Amith Vikram Rangarajan1

  • 1Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.

Biochemistry
|September 26, 2022
PubMed
Summary

Cysteine oxidation impacts protein regulation but is poorly understood. This study analyzes cysteine reactivity, exploring how electrostatics and redox potential influence its oxidation state, and highlights gaps in computational simulation methods.

More Related Videos

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.3K
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

462

Related Experiment Videos

Last Updated: Aug 27, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

1.8K
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.3K
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

462

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Chemistry
  • Chemical Biology

Background:

  • Cysteine side chains exhibit variable oxidation states influenced by environmental pH and redox potential.
  • Cysteine oxidation plays critical regulatory roles in proteins, though its effects are complex and less understood than other post-translational modifications.
  • The impact of cysteine oxidation to sulfenic, sulfinic, and sulfonic acids on protein structure and function is not well-characterized.

Purpose of the Study:

  • To analyze the regulatory role of cysteine reactivity in proteins.
  • To emphasize the interplay between electrostatics and redox potential in determining cysteine oxidation states.
  • To identify underdeveloped research areas in computational approaches for studying cysteine reactivity.

Main Methods:

  • Literature review and analysis of existing research on cysteine oxidation.
  • Exploration of the relationship between environmental factors (pH, redox potential) and cysteine oxidation states.
  • Review of current computational methods for simulating protein systems.

Main Results:

  • Cysteine reactivity is a significant regulatory factor in proteins.
  • Electrostatic interactions and redox potential are key determinants of cysteine oxidation states.
  • Current computational approaches for studying cysteine reactivity via molecular simulations have limitations and underdeveloped areas.

Conclusions:

  • Understanding cysteine oxidation states is crucial for comprehending protein regulation.
  • Further development of computational methods is needed to accurately model cysteine reactivity and its impact on protein function.
  • Interdisciplinary approaches combining electrostatics and redox potential are essential for advancing research in this field.