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Evolution of protein sequences and structures.

T C Wood1, W R Pearson

  • 1Department of Biochemistry, University of Virginia, Charlottesville, VA, 22908, USA.

Journal of Molecular Biology
|August 24, 1999
PubMed
Summary
This summary is machine-generated.

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Protein sequence similarity strongly correlates with structural similarity across diverse protein families. However, the degree of structural change per sequence change varies, suggesting fold information is encoded throughout the protein sequence.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Understanding the relationship between protein sequence and structure is fundamental in molecular biology.
  • Previous studies have explored sequence-structure correlations, but comprehensive analysis across diverse families is ongoing.

Purpose of the Study:

  • To investigate the quantitative relationship between sequence similarity and structural similarity in protein families.
  • To determine factors influencing the variation in structural change relative to sequence change.

Main Methods:

  • Analyzed 36 protein families with known structures and at least five diverse members.
  • Quantified sequence similarity using Smith-Waterman searches.
  • Assessed structural similarity using the DALI structure comparison program.

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Main Results:

  • A strong linear correlation was observed between sequence and structural similarity (r values typically >0.815).
  • Structural mutation sensitivity varied significantly across families, independent of structural class, mutation rate, or protein size.
  • Higher-order terms minimally improved the structure/sequence relationship fit.

Conclusions:

  • Protein fold information is likely encoded across the entire sequence, not just in critical residues.
  • The observed variations in structural mutation sensitivity highlight diverse evolutionary strategies within protein families.