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 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 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 and Protein Structure

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...

Protein Folding

Protein Folding

Protein Folding

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...

You might also read

Related Articles

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

Sort by

Same author

Protein Loop Modeling via the Discretizable Distance Geometry Problem with Hydrogen-Based NMR Constraints.

ACS omega·2026

Same author

Conformal Coordinates for Molecular Geometry: From 3D to 5D.

Journal of computational chemistry·2026

Same author

Influence of Stereochemistry in a Local Approach for Calculating Protein Conformations.

Journal of chemical information and modeling·2024

Same author

A Probabilistic Approach in the Search Space of the Molecular Distance Geometry Problem.

Journal of chemical information and modeling·2024

Same author

A Branch-and-Bound Algorithm for the Molecular Ordered Covering Problem.

Journal of computational biology : a journal of computational molecular cell biology·2024

Same author

Secondary structure assignment of proteins in the absence of sequence information.

Bioinformatics advances·2023

Search research articles

Related Experiment Video

Updated: May 11, 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

A discrete search algorithm for finding the structure of protein backbones and side chains.

Silas Sallaume¹, Simone de Lima Martins, Luiz Satoru Ochi

¹Departamento de Ciência da Computação, Faculdades Thathi, Araçatuba - SP, Brazil. silassallaume@yahoo.com.br

International Journal of Bioinformatics Research and Applications

|May 8, 2013

Summary

This study extends a Branch and Prune algorithm to determine the complete three-dimensional protein structure using sparse distance data from Nuclear Magnetic Resonance (NMR). This advances molecular modeling by reconstructing full protein structures, not just backbones.

More Related Videos

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Related Experiment Videos

Last Updated: May 11, 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

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

Computational Biology
Structural Biology
Biophysics

Background:

Nuclear Magnetic Resonance (NMR) provides limited inter-atomic distance data for proteins.
Determining molecular 3D structure from sparse distances is a key challenge (Molecular Distance Geometry Problem - MDGP).

Purpose of the Study:

To extend the Branch and Prune (BP) algorithm for comprehensive protein structure determination.
To calculate the entire 3D protein structure, beyond just the backbone.

Main Methods:

Utilized a discrete formulation of the Molecular Distance Geometry Problem (MDGP).
Extended a previously developed Branch and Prune (BP) algorithm.

Main Results:

Successfully calculated the complete three-dimensional structure of proteins.
The enhanced algorithm goes beyond predicting only the protein backbone.

Conclusions:

The extended BP algorithm offers a powerful method for full protein 3D structure reconstruction.
This approach enhances the utility of sparse NMR distance data in structural biology.