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Atom depth in protein structure and function.

Alessandro Pintar1, Oliviero Carugo, Sándor Pongor

  • 1Protein Structure and Bioinformatics Group, International Centre for Genetic Engineering and Biotechnology, AREA Science Park, Padriciano 99, 34012 Trieste, Italy. pintar@icgeb.org

Trends in Biochemical Sciences
|November 11, 2003
PubMed
Summary

Atom depth, a measure of protein atom proximity to water, offers insights into protein interiors. This simple geometric descriptor correlates with protein stability, domain size, and residue properties.

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Area of Science:

  • Structural bioinformatics
  • Computational biophysics

Background:

  • Atom depth is a geometrical descriptor of protein interiors.
  • It complements solvent accessible surface area and buried surface area calculations.
  • Depth is easily computed from protein 3D structures.

Purpose of the Study:

  • To highlight the value of atom depth as a protein descriptor.
  • To showcase its correlations with various protein properties.

Main Methods:

  • Computation of atom depth from protein 3D structures.
  • Statistical analysis of correlations between atom depth and other molecular properties.

Main Results:

  • Atom depth is correlated with protein domain size and stability.

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  • It also correlates with hydrophobicity, residue conservation, and amide proton exchange rates.
  • These findings underscore atom depth's utility in understanding protein characteristics.
  • Conclusions:

    • Atom depth is a valuable and easily computable descriptor for protein interiors.
    • It provides complementary information to surface area calculations.
    • Its correlations reveal insights into protein molecular, residue, and atomic properties.