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Related Experiment Videos

Chameleon sequences in the PDB

M Mezei1

  • 1Department of Physiology and Biophysics, Mount Sinai School of Medicine, CUNY, New York, NY 10029, USA.

Protein Engineering
|September 2, 1998
PubMed
Summary
This summary is machine-generated.

Researchers searched the Brookhaven Protein Data Bank for protein sequences adopting both helix and sheet structures. The longest identified sequences capable of forming both conformations were seven residues long.

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Area of Science:

  • Structural biology
  • Protein science
  • Biochemistry

Background:

  • Proteins can adopt various secondary structures, including alpha-helices and beta-sheets.
  • Understanding conformational flexibility is crucial for protein function and evolution.
  • The Brookhaven Protein Data Bank (PDB) is a primary repository for protein structural data.

Purpose of the Study:

  • To identify protein sequence segments capable of adopting both alpha-helix and beta-sheet conformations.
  • To determine the maximum length of such amphiforming sequences within the PDB.

Main Methods:

  • Bioinformatic search of the Brookhaven Protein Data Bank (PDB).
  • Analysis of protein sequences for regions exhibiting dual secondary structure propensity (helix and sheet).

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  • Identification and measurement of the longest sequences displaying this characteristic.

    • Main Results:

    • Identified protein sequence segments capable of existing in both helix and sheet conformations.
    • The longest such identified sequences were found to be seven residues in length.

    Conclusions:

    • Short protein segments (up to seven residues) can possess the intrinsic ability to form both alpha-helical and beta-sheet structures.
    • This conformational plasticity in short sequences may have implications for protein folding, dynamics, and function.