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A method for multiple superposition of structures.

A Shapiro1, J D Botha, A Pastore

  • 1Department of Mathematics, Applied Mathematics and Astronomy, University of South Africa, Pretoria.

Acta Crystallographica. Section A, Foundations of Crystallography
|January 1, 1992
PubMed
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This study presents a method for aligning multiple protein structures to understand molecular evolution and NMR data. The technique finds optimal transformations for superposing protein conformations with specified atom correspondence.

Area of Science:

  • Structural biology
  • Computational biology
  • Molecular evolution

Background:

  • Analyzing families of protein structures is crucial for interpreting Nuclear Magnetic Resonance (NMR) structure determination results.
  • Understanding protein conformational evolution requires methods to compare multiple related structures.

Purpose of the Study:

  • To present a computational method for superposing an arbitrary number of protein structures.
  • To enable the analysis of protein structure families and their evolutionary relationships.

Main Methods:

  • The study discusses a least-squares method for calculating transformations.
  • This method requires specified atom-to-atom correspondence between structures.

Main Results:

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  • The method allows for the mutual superposition of multiple protein structures.
  • It provides a quantitative way to compare protein conformations.

Conclusions:

  • The developed method is valuable for analyzing NMR data and studying molecular evolution.
  • It offers a robust approach to structural alignment for comparative analysis.