Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein-Protein Interfaces

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein Organization

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 Organization

Protein Organization

Protein and Protein Structures

Protein and Protein Structures

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...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

You might also read

Related Articles

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

Sort by

Same author

sweelin®, a novel sweet protein, does not affect blood glucose and insulin levels - a double-blind, crossover, randomized study.

Food chemistry·2026

Same author

Structural basis for ADAM17 activation by the iRhom1 pseudoprotease.

Cell reports·2026

Same author

RNase A is inhibited by the cysteine-rich protein thionein but not by the metal-containing form metallothionein.

Molecular and cellular biochemistry·2026

Same author

Terminal-Directed Supramolecular Liquid Crystal Formation by Designed Coiled-Coil Interparticle Stacking.

ACS nano·2026

Same author

Patchy peptide particles for pH-responsive assembly into liquid crystals or lattices.

Science (New York, N.Y.)·2026

Same author

Electrostatic Coassembly of Coiled-Coil Peptide Bundlemers with Complementary Charges into Porous 2D Lattices.

Journal of the American Chemical Society·2025

Search research articles

Related Experiment Video

Updated: Jun 6, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Theoretical and computational protein design.

Ilan Samish¹, Christopher M MacDermaid, Jose Manuel Perez-Aguilar

¹Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Annual Review of Physical Chemistry

|December 7, 2010

Summary

Computational protein design identifies novel sequences for specific structures and functions. Sophisticated methods enable the creation of new proteins and functionalities, advancing biological and nonbiological applications.

More Related Videos

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

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

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Related Experiment Videos

Last Updated: Jun 6, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

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

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

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Biochemistry and Molecular Biology
Computational Biology
Protein Engineering

Background:

Designing proteins with specific structures and functions from vast sequence possibilities is a complex challenge.
Protein structure and function depend on intricate intermolecular forces and amino acid interactions.
Existing methods for sequence characterization aid in designing novel proteins.

Purpose of the Study:

To discuss developments in computational protein design.
To highlight recent accomplishments in protein sequence identification.
To explore applications of designed proteins in biological and nonbiological contexts.

Main Methods:

Utilizing sophisticated computational methods to characterize protein sequences.
Analyzing intermolecular forces and amino acid interactions for structure prediction.
Developing algorithms for identifying sequences consistent with predetermined structures.

Main Results:

Advancements in computational tools have been made for protein design.
Successful redesign of existing proteins has been achieved.
Novel protein functionalities and nonbiological applications have been designed.

Conclusions:

Computational protein design is a rapidly advancing field.
Sophisticated methods facilitate the creation of proteins with targeted properties.
The technology holds promise for diverse applications, including novel functionalities and nonbiological uses.