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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
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 Organization01:24

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.
Protein Organization01:13

Protein Organization

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Protein Organization01:13

Protein Organization

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Related Experiment Video

Updated: Jun 24, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for

Sarah A Fowler1, Helen E Blackwell

  • 1Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706-1322, USA.

Organic & Biomolecular Chemistry
|April 4, 2009
PubMed
Summary
This summary is machine-generated.

N-substituted glycine oligomers, or peptoids, show promise as therapeutics. Understanding peptoid structure-function relationships is key to designing novel, functional peptoids for various applications.

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Last Updated: Jun 24, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

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Published on: November 2, 2011

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Published on: November 21, 2013

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

  • Synthetic chemistry
  • Biochemistry
  • Materials science

Background:

  • N-substituted glycine oligomers (peptoids) are increasingly recognized for their biological versatility and therapeutic potential.
  • A central focus in peptoid research is elucidating the link between their structural conformation and functional activity.
  • Current understanding of peptoid structure-function relationships is often established post-synthesis and characterization.

Purpose of the Study:

  • To review recent advancements in understanding peptoid structure-function relationships.
  • To highlight how elucidated folding guidelines can enable de novo design of functional peptoids.
  • To explore the expanding landscape of peptoid biological activities.

Main Methods:

  • Literature review of peptoid research from the past five years.
  • Analysis of studies correlating peptoid folding and biological function.
  • Synthesis and characterization of peptoid structures (implied).

Main Results:

  • Specific structure-function correlations in peptoids have been identified.
  • The necessity of folded versus unstructured peptoids varies by application.
  • Emerging guidelines for peptoid folding are being established.

Conclusions:

  • Peptoid structure-function relationships are critical for their application and design.
  • Further elucidation of folding principles will facilitate the de novo design of functional peptoids.
  • The expanding knowledge base promises new therapeutic and research tools.