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Related Concept Videos

What are Proteins?01:28

What are Proteins?

Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
What are Proteins?01:55

What are Proteins?

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.
Protein Organization01:13

Protein Organization

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 Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 10, 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

The subsequence composition of polypeptides.

Alberto Apostolico1, Fabio Cunial

  • 1College of Computing, Georgia Institute of Technology, Atlanta, GA 30318, USA. axa@cc.gatech.edu

Journal of Computational Biology : a Journal of Computational Molecular Cell Biology
|July 30, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces new parameters to analyze polypeptide structure and randomness using subsequences, not substrings. These measures reveal underlying biochemical information and differentiate real polypeptides from random sequences.

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Last Updated: Jun 10, 2026

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

  • Bioinformatics
  • Computational Biology
  • Biophysics

Background:

  • Quantitative analysis of biosequences is crucial for understanding biological function and evolution.
  • Previous studies focused on substrings, revealing limited compressibility in biosequences compared to random strings.
  • Distinguishing biologically relevant sequences from random ones remains a challenge.

Purpose of the Study:

  • To develop novel parameters for assessing polypeptide structure and randomness.
  • To analyze polypeptides based on subsequence vocabulary rather than substring composition.
  • To explore the relationship between these parameters and biochemical diversity.

Main Methods:

  • Introduction of new parameters based on subsequence vocabulary.
  • Analysis of polypeptide sequences and their random permutations.
  • Application of these parameters across biochemically diverse polypeptides.

Main Results:

  • The new parameters effectively capture structural and functional information in polypeptides.
  • These parameters exhibit specific interrelationships across various polypeptide types.
  • Subsequence measures distinguish natural amino acid strings from their random permutations, with most random permutations clustering along linear loci.

Conclusions:

  • Subsequence-based analysis offers a novel approach to quantifying biosequence information content.
  • The identified parameters provide insights into the inherent structure and randomness of polypeptides.
  • This method advances the quantitative study of biological sequences and their underlying principles.