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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Conservation of Protein Domains02:26

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Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

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Published on: January 8, 2019

Analysis of protein chameleon sequence characteristics.

Amine Ghozlane1, Agnel Praveen Joseph, Aurelie Bornot

  • 1Equipe de Bioinformatique Genomique et Moleculaire (EBGM), INSERM UMR-S 726, DSIMB, Universite Paris Diderot- Paris 7, Institut National de Transfusion Sanguine (INTS), 6, rue Alexandre Cabanel, 75739 Paris cedex 15, France.

Bioinformation
|September 18, 2009
PubMed
Summary

Chameleon sequences, protein fragments lacking a fixed secondary structure, exhibit complex conformational preferences. Analysis reveals many favor coil states or multiple structures like alpha-helices and beta-strands.

Keywords:
chameleon sequencesecondary structuresstructural characteristics

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Area of Science:

  • Protein structure and dynamics
  • Biochemistry of protein folding
  • Molecular basis of disease

Background:

  • Protein structural conversions, like alpha-helix to beta-strand, often involve significant tertiary structure changes.
  • Amyloidogenic protein self-assembly into fibrils is linked to diseases such as Alzheimer's disease.
  • Chameleon sequences are protein fragments with ambiguous secondary structure preferences.

Purpose of the Study:

  • To analyze chameleon sequences on a large scale.
  • To estimate the propensity of chameleon sequences for different local structural states (alpha-helices, beta-strands, coils).
  • To understand the complexity of chameleon sequence behavior.

Main Methods:

  • Large-scale analysis of chameleon sequences.
  • Estimation of conformational propensities based on amino acid composition.
  • Prediction of secondary structure based on local sequence neighborhood.

Main Results:

  • Over 25% of chameleon sequences show a preference for the coil state over regular secondary structures.
  • Approximately 50% of chameleon sequences exhibit preference for both alpha-helix and beta-sheet conformations.
  • The remaining chameleon sequences favor either alpha-helix or beta-sheet conformations.

Conclusions:

  • Chameleon sequences display complex conformational preferences, often favoring coil states or multiple secondary structures.
  • Understanding these propensities is crucial for predicting protein folding and assembly.
  • This complexity may offer insights into protein misfolding diseases.