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Published on: September 15, 2010
Protein folds: molecular systematics in three dimensions.
1Department of Chemistry and E. O. Lawrence Berkeley National Laboratory, University of California, Berkeley 94720, USA.
Cellular and Molecular Life Sciences : CMLS
|March 7, 2001
Summary
Protein structure determination has revealed common principles in protein folding and evolution. A limited number of protein folds accommodate many genes, suggesting a finite "fold universe" is near discovery.
Area of Science:
- Structural biology
- Bioinformatics
- Evolutionary biology
Background:
- Advances in protein structure determination methods have generated substantial structural data.
- Approximately 500 distinct protein folds have been characterized, representing a significant portion of known globular protein structures.
Purpose of the Study:
- To identify unifying principles governing protein structure and evolution.
- To explore the diversity and distribution of protein folds within the broader protein universe.
Main Methods:
- Analysis of a large dataset of determined protein structures.
- Statistical examination of topological arrangements and sequence-accommodation capacities of protein folds.
Main Results:
- Discovery of a highly skewed distribution in secondary structure element arrangements, favoring common connectivities.
- Identification of a skewed distribution in the capacity of folds to accommodate unrelated protein sequences.
- Evidence suggests the total number of protein folds is significantly less than the number of genes.
Conclusions:
- The protein fold universe is dominated by a small number of highly versatile folds, termed "giant attractors."
- The complete set of basic protein folds is likely to be determined soon.
- This comprehensive understanding will form the basis for understanding organism-wide biochemical and cellular functions.
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