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 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...

Protein Folding

Protein Folding

Newman Projections

Newman Projections

Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as conformers.

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

You might also read

Related Articles

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

Sort by

Same author

Vestibular function analyzed by a video head impulse test in patients with idiopathic sudden sensorineural hearing loss associated with vertigo.

Acta oto-laryngologica·2026

Same author

Cardiac Allograft Vasculopathy: 5-Year Longitudinal Morphological Changes Assessed by Optical Coherence Tomography.

JACC. Asia·2026

Same author

Cerebrospinal fluid soluble protein tyrosine phosphatase receptor type Z detected with human natural killer-1 antibody as a practical biomarker for glioma diagnosis.

Neuro-oncology advances·2026

Same author

Association of elevated cyclic GMP levels with hemodynamic changes in HFrEF patients treated with sacubitril/valsartan and vericiguat: a pilot study.

International journal of cardiology. Heart & vasculature·2026

Same author

Increased Cerebral Blood Flow in the Anterior Cingulate Cortex and Plasma Noradrenaline Level During Cardiac Pacemaker Stimulation.

Circulation journal : official journal of the Japanese Circulation Society·2026

Same author

Linking the heart-eye-brain axis: Ocular and cerebral blood flow changes after catheter ablation in atrial fibrillation.

Heart rhythm·2026

Search research articles

Related Experiment Video

Updated: Jul 19, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

Mathematical folding of node chains in a molecular network.

Hideaki Suzuki¹

¹Kobe Advanced ICT Research Center (KARC), National Institute of Information and Communications Technology (NICT), Japan. hsuzuki@nict.go.jp

|October 19, 2006

Summary

This study introduces network artificial chemistry (NAC) to build machines from genetic data. Algorithms transform node chains into control-flow clusters, demonstrating functions like splitase and replicase.

More Related Videos

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Published on: August 15, 2018

Related Experiment Videos

Last Updated: Jul 19, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Published on: August 15, 2018

Area of Science:

Artificial Chemistry
Computational Biology
Systems Biology

Background:

Network Artificial Chemistry (NAC) provides a framework for studying emergent behaviors in complex systems.
Understanding the genotype-phenotype relationship is crucial for artificial life and synthetic biology.

Purpose of the Study:

To propose a novel method for constructing phenotypic machines from genotypic information within the NAC framework.
To demonstrate the functionality of these machines using specific examples.

Main Methods:

Genotypic information represented as node chains with symbol data.
An algorithm implemented for chain agglomeration, tangling, and folding into node clusters.
Development of control-flow clusters acting as machines.

Main Results:

Successful construction of phenotypic machines from genotypic sequences.
Demonstration of two functional control-flow clusters: splitase and replicase.
Validation of the proposed method for genotype-to-phenotype mapping.

Conclusions:

The proposed NAC method effectively translates genotypic information into functional phenotypic machines.
The developed control-flow clusters offer a novel approach to computational modeling in artificial chemistry.
Future research can explore diverse machine functionalities and applications.