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

Ionic Crystal Structures02:42

Ionic Crystal Structures

16.9K
Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...
16.9K
Structural Protein Function01:56

Structural Protein Function

29.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
29.9K
Structural Protein Function01:56

Structural Protein Function

3.2K
3.2K
Fruit Development, Structure, and Function01:58

Fruit Development, Structure, and Function

25.1K
Fruits form from a mature flower ovary. As seeds develop from the ovules contained within, the ovary wall undergoes a series of complex changes to form fruit. In some fruits, such as soybeans, the ovary wall dries; in other fruits, such as grapes, it remains fleshy. In some cases, organs other than the ovary contribute to fruit formation; such fruits are called accessory fruits.
25.1K
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

5.4K
There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
5.4K
Structure and Function of Platelets01:18

Structure and Function of Platelets

3.2K
The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
Platelets are continually replenished, circulating in the bloodstream for 9-12 days before being removed by phagocytes, primarily in the spleen. A microliter of circulating blood contains between 150,000 and 450,000...
3.2K

You might also read

Related Articles

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

Sort by
Same author

Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochrome <i>b</i><sub>5</sub>.

Physical chemistry chemical physics : PCCP·2024
Same author

Selective steroidogenic cytochrome P450 haem iron ligation by steroid-derived isonitriles.

Communications chemistry·2023
Same author

Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450<sub>cam</sub> (CYP101A1).

Biochemistry·2022
Same author

A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I).

Biochemistry·2020
Same author

Substrate recognition by two different P450s: Evidence for conserved roles in a common fold.

Scientific reports·2017
Same author

The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.

Chemical reviews·2017

Related Experiment Video

Updated: Jan 25, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

30.6K

What Your Crystal Structure Will Not Tell You about Enzyme Function.

Thomas C Pochapsky, Susan Sondej Pochapsky

    Accounts of Chemical Research
    |April 30, 2019
    PubMed
    Summary

    Enzyme dynamics are crucial for function, but traditional methods like X-ray crystallography miss key conformations. Solution NMR, using specialized techniques for large enzymes like cytochrome P450s, reveals these hidden structural changes essential for substrate specificity and catalysis.

    More Related Videos

    Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
    11:31

    Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

    Published on: November 30, 2018

    7.9K
    Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
    10:45

    Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

    Published on: March 20, 2021

    8.8K

    Related Experiment Videos

    Last Updated: Jan 25, 2026

    Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
    22:00

    Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

    Published on: November 21, 2010

    30.6K
    Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
    11:31

    Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

    Published on: November 30, 2018

    7.9K
    Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
    10:45

    Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

    Published on: March 20, 2021

    8.8K

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Biophysics

    Background:

    • Enzyme function relies on dynamic structural changes, including substrate binding and transition state stabilization.
    • X-ray crystallography captures static enzyme conformations, potentially missing functionally relevant dynamics.
    • Solution Nuclear Magnetic Resonance (NMR) offers a non-perturbing method to study enzyme dynamics in solution.

    Purpose of the Study:

    • To investigate the structural and dynamic aspects of function in the cytochrome P450 monooxygenase superfamily using NMR.
    • To develop specialized NMR approaches for large enzymes like P450s, enabling resonance assignments and analysis of dynamic processes.
    • To understand how enzyme structure and dynamics dictate substrate-product specificity in P450-catalyzed reactions.

    Main Methods:

    • Utilized solution NMR spectroscopy to study enzyme dynamics under various conditions (ligand binding, redox state changes).
    • Developed specialized techniques for sequential resonance assignments in large enzymes.
    • Employed residual dipolar couplings (RDCs) and restrained molecular dynamics (MD) simulations ('soft annealing') to characterize conformational ensembles.
    • Validated NMR findings through site-directed mutagenesis, spectroscopic assays, and activity measurements.

    Main Results:

    • Identified cryptic conformational changes in P450s upon substrate and redox partner binding, not evident from crystal structures.
    • Demonstrated the functional relevance of these dynamic conformational changes.
    • Observed that identified P450 dynamics may be generalizable across the superfamily, offering insights for enzyme engineering.

    Conclusions:

    • Solution NMR is a powerful tool for characterizing enzyme dynamics, complementing X-ray crystallography.
    • Cytochrome P450s exhibit functionally relevant conformational dynamics that are critical for their broad substrate scope and specificity.
    • These findings provide a foundation for understanding and engineering P450 enzymes, including medically relevant human isoforms.