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Proc Natl Acad Sci U S A. 2004 Sep 14;101(37):13460-5. Epub 2004 Sep 3.

Molecular dimension explored in evolution to promote proteomic complexity.

Author information

1
Indiana University School of Informatics and Indiana Genomics Initiative Center for Computational Biology and Bioinformatics, Indiana University Medical School, 714 North Senate Avenue, Indianapolis, IN 46202, USA. arfernan@iupui.edu

Abstract

The architecture of present-day protein interaction networks depends on how protein associations evolved. Here, we explore how and why evolution-related mutations influence protein structure to promote protein associations, and thereby network development. We specifically address two questions: (i) How can protein folds remain conserved while proteins accommodate new binding partnerships as genes duplicate? (ii) What is the structural/molecular basis for hub proteins being the most likely to acquire new connections? The answers stem from the examination of the structure wrapping, or protection from water attack. Wrapping is shown to be a crucial consideration in the exploration and evolution of proteomic interactivity.

PMID:
15347802
PMCID:
PMC518779
DOI:
10.1073/pnas.0405585101
[Indexed for MEDLINE]
Free PMC Article

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