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CORRELATED MUTATIONS IN SELECTED PROTEIN FAMILIES

Abstract

Four different protein families (two proteinase inhibitor families, myoglobins and lysozymes) were surveyed for correlated mutations with respect to the position distance and their significance in structure stabilization and biological activity. They were chosen for this study in order to verify the currently admitted model of mutational correlation relationship with respect to spatial contact of the residues and contribution in protein biological activity. There was observed high contribution of spatially dispersed residues (which are also not involved in the protein active center) in mutational correlation. Because of the significantly large distance between correlated positions these cases do not correspond explicitly to any mechanism included in current hypotheses. It is suggested that the role of residue spatial contact in structure preservation, intermolecular interaction and active site rescue mechanisms only partially explains the correlation phenomenon.

Keywords:

protein sequence, multiple alignment, tertiary structure, mutational correlation, genetic semihomology algorithm

Details

Issue
Vol. 6 No. 3 (2002)
Section
Research article
Published
2002-09-30
Licencja:
Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Author Biography

JACEK LELUK,
University of Wroclaw, Institute of Biochemistry and Molecular Biology; University of Warsaw, Interdisciplinary Centre for Mathematical and Computational Modeling (ICM)



Authors

  • JACEK LELUK

    University of Wroclaw, Institute of Biochemistry and Molecular Biology; University of Warsaw, Interdisciplinary Centre for Mathematical and Computational Modeling (ICM)
  • MONIKA SOBCZYK

    University of Wroclaw, Institute of Biochemistry and Molecular Biology
  • ŁUKASZ BECELLA

    University of Wroclaw, Institute of Biochemistry and Molecular Biology

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