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Local flexibility in molecular function paradigm.
Jag Bhalla1, Geoffrey B Storchan, Caitlin M MacCarthy
1Biochemistry and Molecular & Cellular Biology, Georgetown University School of Medicine, Washington, DC 20007, USA.
Molecular & Cellular Proteomics : MCP
|March 31, 2006
Summary
Biological macromolecules need flexibility for function. This study reveals that protein flexibility varies by function, with gene regulators being more flexible than oxygen transporters.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Traditionally, tightly packed 3D structures were considered essential for macromolecular function.
- Emerging evidence highlights the critical role of molecular flexibility in protein activity.
Purpose of the Study:
- To investigate the relationship between protein structure, flexibility, and function.
- To assess the percentage of flexible residues in proteins across different functional categories.
Main Methods:
- Analysis of high-resolution protein structures.
- Secondary structure assessment to characterize local polypeptide chain flexibility.
- Phylogenetic comparison of protein families.
Main Results:
- Proteins in functional states contain 20-70% flexible residues.
- Gene regulation proteins (e.g., transcription factors) exhibit >60% flexible residues.
- Oxygen transporters are relatively rigid, with ~30% flexible residues.
- Local flexibility increases with organism complexity and is higher in extracellular proteins.
Conclusions:
- Molecular flexibility is a key determinant of protein function across diverse categories.
- The degree of protein flexibility correlates with biological complexity and cellular environment.
- Understanding protein flexibility is crucial for comprehending biological processes.