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Protein folding: search for basic physical models.

Ivan Y Torshin1, Robert W Harrison

  • 1Department of Biology, Georgia State University, Atlanta, Georgia 30303, USA. biotiy@suez.cs.gsu.edu

Thescientificworldjournal
|August 16, 2003
PubMed
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Understanding protein folding requires exploring fundamental physical forces. This review examines physical models linking amino acid sequences to protein structures, crucial for genomics.

Area of Science:

  • Biophysics
  • Computational Biology
  • Molecular Biology

Background:

  • Protein folding, the process by which a linear polypeptide chain adopts a unique three-dimensional structure, remains a central question in science.
  • Current models often overlook the fundamental physical forces governing in vitro folding and the rapid, specific nature of protein architecture formation.

Purpose of the Study:

  • To review physical models that directly link polypeptide sequence to tertiary structure.
  • To highlight the importance of fundamental physical forces (electrostatics, Van Der Waals) in protein folding.
  • To explore the potential of these models for developing advanced computational techniques.

Main Methods:

  • Review of existing physical models of protein folding.
  • Analysis of the role of fundamental physical forces in protein structure formation.

Related Experiment Videos

  • Discussion of computational approaches derived from physical principles.

    • Main Results:

    • Few current models explicitly incorporate basic physical forces like electrostatics and Van Der Waals forces.
    • Existing statistical and thermodynamic approaches have limitations in explaining the speed and specificity of protein folding.
    • Physical models offer a more direct link between amino acid sequence and tertiary structure.

    Conclusions:

    • Incorporating fundamental physical forces into protein folding models is essential for a comprehensive understanding.
    • Simple physical models can lead to highly effective computational techniques for genomics.
    • Further research into physical models can advance our ability to predict and engineer protein structures.