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Related Concept Videos

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 Folding01:22

Protein Folding

Overview
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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...
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.

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Related Experiment Video

Updated: Jun 4, 2026

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

Ionic polypeptides with unusual helical stability.

Hua Lu1, Jing Wang, Yugang Bai

  • 1Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Nature Communications
|February 24, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed ultra-stable, water-soluble helical polypeptides by extending charged amino-acid side chains. This strategy enhances helical stability in peptides, overcoming challenges in medicine and biotechnology.

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

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Last Updated: Jun 4, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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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

Area of Science:

  • Biochemistry
  • Polymer Science
  • Biotechnology

Background:

  • Water-soluble peptides with stable helical conformations are crucial in science, medicine, and biotechnology.
  • Incorporating charged residues for solubility often reduces helical stability due to charge repulsion and disrupted hydrogen bonding.

Purpose of the Study:

  • To design and synthesize water-soluble, ultra-stable alpha-helical polypeptides.
  • To overcome the common challenge of reduced helical stability when incorporating charged amino acids.

Main Methods:

  • Elongating charge-containing amino-acid side chains to position charges away from the polypeptide backbone.
  • Designing and synthesizing novel water-soluble polypeptides with long, charged side chains and functional moieties.

Main Results:

  • Achieved unusual helical stability in designed polypeptides across various environmental conditions.
  • Demonstrated stability against changes in pH, temperature, and denaturing reagents.
  • Successfully produced water-soluble, ultra-stable alpha-helical polypeptides.

Conclusions:

  • Elongating charged side chains is an effective strategy for creating stable, water-soluble helical polypeptides.
  • This approach enhances peptide stability, broadening their utility in medicine and biotechnology.
  • The designed polypeptides exhibit remarkable resilience to environmental stressors.