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                                             BIOINFORMATICS COLLOQUIUM
						College of Science
                                              George Mason University
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	                       Polymeric aspects of structure-function relationships
						 
                                               Olga Tcherkasskava

				Department of Biochemistry and Molecular Biology 
				    Georgetown University School of Medicine

Abstract:
Given the rapid growth in biological sequence information, immediate efforts are 
focused on producing structural information for new proteins with high throughput.  
Though the number of structural techniques increases steadily (i.e., synchrotron 
X-ray crystallography, micro-crystallography, solid state NMR, cryo-electron 
microscopy), determining a complete protein structure is still a long, involved 
process. Yet, the functionally competent protein molecules may be partly (e.g., 
molten globules or denatured compact states) or largely unfolded (e.g., natively 
unfolded proteins).  It is essential, therefore, to develop bioinformatic tools 
that would aid greatly our understanding "structure-function" relationships and 
could be useful for structure prediction/determination agenda. I will demonstrate 
that conventional biophysical characteristics of the native structures (such as 
effective size, thermodynamic flexibility, etc) underline various aspects of 
structure-function relationships that have previously been overlooked.

REFERENCES
1.  Bhalla, J., Storchan, G., MacCarthy, C.M., Uversky, V.N., and Tcherkasskaya, O.  Local 
Flexibility in Structure-Function Paradigm.  Molecular and Cellular Proteomics  2006 5(7):1212-1223.
2.  Tcherkasskaya, O. and Uversky, V.N.  Polymeric aspects of protein folding: A brief overview. 
Protein and Peptide Letters 2003, 10 (3): 239-245.
3.  Tcherkasskaya, O., Davidson E.A., and Uversky, V.N.  Biophysical Constraints for Protein 
Structure Prediction.  J. Proteome Res. 2003, 2: 37-42.
4.  Tcherkasskaya, O., and Uversky V.N.  Denatured collapse states in protein folding: Example 
of apoomyoglobin.  Proteins: Structure, Function, and Genetics  2001, 44:244-254.