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

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 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.

You might also read

Related Articles

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

Sort by

Same author

Novel Prion Protein Gene (<i>PRNP)</i> Variants in Wild Montana Mule Deer.

bioRxiv : the preprint server for biology·2026

Same author

Mutation of Pro76 affects the dynamics of Ω-loop D of yeast Iso-1-cytochrome c: Application of gated electron transfer.

Journal of inorganic biochemistry·2026

Same author

Physical and functional effects of substituting coevolved residues from Ω-loop C of yeast Iso-1-cytochrome c into human cytochrome c.

Journal of inorganic biochemistry·2025

Same author

Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength.

Journal of inorganic biochemistry·2024

Same author

Effect of proline content and histidine ligation on the dynamics of Ω-loop D and the peroxidase activity of iso-1-cytochrome c.

Journal of inorganic biochemistry·2024

Same author

High-Accuracy Prediction of Stabilizing Surface Mutations to the Three-Helix Bundle, UBA(1), with EmCAST.

Journal of the American Chemical Society·2023

Search research articles

Related Experiment Video

Updated: May 28, 2026

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

Residual structure in unfolded proteins.

Bruce E Bowler¹

¹Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Dynamics, The University of Montana, Missoula, MT 59812, USA. bruce.bowler@umontana.edu

Current Opinion in Structural Biology

|October 8, 2011

Summary

Unfolded proteins contain residual structures, not just random coils. Studying these structures offers insights into the protein folding code and long-range interactions.

Area of Science:

Biochemistry
Structural Biology
Protein Folding Dynamics

Background:

The denatured state ensemble (DSE) of unfolded proteins was historically viewed as an energetically featureless random coil.
Emerging evidence indicates the presence of transient, flickering residual structures within the DSE.
Understanding these residual structures is crucial for deciphering the fundamental principles of protein folding.

Purpose of the Study:

To review recent advancements in characterizing the denatured state ensemble (DSE) of unfolded proteins.
To explore the nature of DSE collapse under folding conditions.
To highlight progress in quantifying residual structure stability and identifying key residues involved.

Main Methods:

Review of recent experimental and computational studies on protein DSE.

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

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Related Experiment Videos

Last Updated: May 28, 2026

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

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

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

Published on: July 16, 2017

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Analysis of techniques for quantifying residual structure stability.

Examination of methods for detecting long-range interactions in unfolded proteins.

Main Results:

The DSE is not a featureless random coil but contains significant residual structure.
Advances have been made in quantifying the stability and identifying residues involved in this structure.
New methods allow for the detection of long-range interactions within the DSE.

Conclusions:

Residual structures in the DSE play a critical role in protein folding.
Further investigation into DSE structure can unlock secrets of the protein folding code.
Recent advances provide powerful tools for studying these complex protein dynamics.