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 Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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...
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

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.
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...

You might also read

Related Articles

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

Sort by
Same author

Europium Coordination Structure in Peptide Complexes Resolved with Simulation and X-ray Absorption Spectroscopy.

The journal of physical chemistry. B·2026
Same author

Ti-15Zr-5.5Cu: A dental titanium alloy with robust antibacterial activity and superior corrosion resistance.

iScience·2026
Same author

Supramolecular Encapsulation of [Nd(NO<sub>3</sub>)<sub>6</sub>]<sup>3-</sup> by <i>dpat</i> Retained in Acetonitrile.

Inorganic chemistry·2026
Same author

Successful treatment of a complex Skene's gland cyst: a case report.

Therapeutic advances in urology·2025
Same author

Electron-withdrawing groups as property tuners in functionalized terpyridine-based ligands in Eu(III) and Tb(III) complexes.

Dalton transactions (Cambridge, England : 2003)·2025
Same author

Multi-omics analysis identified LGALS1 (Galectin-1) as a novel therapeutic target for clear cell renal cell carcinoma via targeting epithelial or endothelial cells.

Discover oncology·2025

Related Experiment Video

Updated: Jun 12, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Thioesterases: a new perspective based on their primary and tertiary structures.

David C Cantu1, Yingfei Chen, Peter J Reilly

  • 1Department of Chemical and Biological Engineering, Iowa State University, Ames, Iowa 50011, USA.

Protein Science : a Publication of the Protein Society
|May 28, 2010
PubMed
Summary
This summary is machine-generated.

This study reclassifies thioesterases (TEs) into 23 distinct families and four clans based on structural and sequence analysis. The ThYme database offers a new classification for these crucial enzymes.

More Related Videos

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Related Experiment Videos

Last Updated: Jun 12, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Thioesterases (TEs) are enzymes with diverse substrates, currently classified under EC 3.1.2.1-EC 3.1.2.27, with many unclassified.
  • Existing classifications do not fully capture the evolutionary and structural relationships among TEs.
  • Analysis of primary and tertiary structures is crucial for understanding TE diversity and function.

Purpose of the Study:

  • To re-evaluate and redefine thioesterase families and clans using structural and sequence-based criteria.
  • To establish a new classification system for thioesterases.
  • To present the updated ThYme database for thioesterase research.

Main Methods:

  • Utilized strong primary sequence conservation of experimentally validated proteins as the primary classification criterion.
  • Verified classifications through tertiary structure superpositions, mechanistic studies, and catalytic residue analysis.
  • Integrated data on substrate specificity (e.g., CoA, ACP, glutathione) and protein interactions.

Main Results:

  • Identified 23 thioesterase families largely unrelated by primary structure.
  • Established four clans encompassing 12 thioesterase families, revealing distant evolutionary relationships.
  • Developed the ThYme database, providing a novel classification of TE structures, families, and clans.

Conclusions:

  • The new classification based on structural and sequence data offers a more accurate representation of thioesterase evolution and relationships.
  • TEs exhibit diverse folds and mechanisms, even within the same family, and convergent evolution is evident in different families with similar structures.
  • The ThYme database serves as a valuable, updated resource for researchers studying thioesterases and their functions.