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Related Concept Videos

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...
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 Folding01:22

Protein Folding

Overview
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

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Binary classification of protein molecules into intrinsically disordered and ordered segments.

Satoshi Fukuchi1, Kazuo Hosoda, Keiichi Homma

  • 1Center for Information Biology & DNA Data Bank of Japan, National Institute of Genetics, Yata 1111, Mishima, Shizuoka 411-8540, Japan. sfukuchi@genes.nig.ac.jp

BMC Structural Biology
|June 23, 2011
PubMed
Summary
This summary is machine-generated.

A new method classifies protein regions into structural domains (SDs) and intrinsically disordered (ID) regions, revealing that 35% of the human proteome is intrinsically disordered. This provides key insights into protein architecture and function.

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Area of Science:

  • Proteomics
  • Structural Biology
  • Bioinformatics

Background:

  • Many protein regions lack structural domain (SD) assignments, potentially representing novel SDs or intrinsically disordered (ID) regions.
  • Proteins, particularly in eukaryotes, contain substantial ID regions that can be inferred from amino acid sequences.
  • A combined approach for SD and ID region assignment is needed to characterize proteomes comprehensively.

Purpose of the Study:

  • To develop and apply a method that classifies entire protein sequences into structural domains (SDs) and intrinsically disordered (ID) regions.
  • To determine the genome-wide fractions of SDs and ID regions in the human proteome and other model organisms.
  • To investigate the relationship between ID regions and protein function, localization, and post-translational modifications.

Main Methods:

  • Utilized the previously developed DICHOT system for classifying protein sequences into SDs and ID regions.
  • Applied DICHOT to the human proteome and proteomes of other model organisms.
  • Analyzed the distribution of ID regions across different subcellular localizations and their association with post-translational modifications and alternative splicing.

Main Results:

  • The human proteome comprises 35% residue-wise ID regions, 52% SDs with known structures, and 13% novel cryptic domains.
  • Eukaryotic proteomes exhibit higher ID content than prokaryotic proteomes.
  • ID regions are enriched in nuclear proteins, and preferentially contain phosphorylation and O-linked glycosylation sites, and are associated with alternative splicing.

Conclusions:

  • The DICHOT method enables complete classification of protein regions into SDs and ID regions, yielding comprehensive genome-wide statistics.
  • These findings provide fundamental information for understanding protein structural organization and function.
  • The data and method are publicly available for further research.