Disorder in Protein Structure and Function

Keith Dunker, Charles Kissinger & Eugene Shakhnovich


Certain regions within proteins and some entire proteins are not ordered into unique structure, but rather exist as ensembles of structures. There is a growing awareness that these 'disordered' or 'non-folding' proteins often carry out important biological functions, indeed that the lack of folding into a fixed structure is required for function. This tutorial will provide information regarding the theoretical basis of non-folding proteins, laboratory methods used to characterize disorder, important examples of natively disordered proteins, and information regarding the identified functions and advantages associated with disordered as opposed to ordered protein structure.

Biographical Sketches

A. Keith Dunker
Department of Biochemistry,
Washington State University,
Pullman, WA 99164-4660
telephone: 509 335-5322
facsimile: 509 335-9688
e-mail: dunker@mail.wsu.edu

Research Interests: Dr. Dunker's research from 1965 until now has centered on protein structure and function, especially as regards to virus capsid structure and assembly. In the late 1980s he became began research on the relationship between amino acid sequence and protein structure, publishing his first paper in this area in 1990. Recently he began collaborations with Zoran Obradovic of the WSU Computer Science Department on the prediction of protein disorder from amino acid sequence.

Charles Kissinger
Agouron Pharmaceuticals, Inc.
3565 General Atomics Court
San Diego, CA 92121
telephone: 619-622-7930
facsimile: 619-622-7999
e-mail: crk@agouron.com

Research Interests: Dr. Kissinger's research has focused primarily on understanding the structural basis for molecular recognition, including protein-protein, protein-nucleic acid, and protein-ligand interactions. His current work involves the application of x-ray crystallography to structure-based drug design and the development of new methods for crystallographic structure determination.

Eugene Shakhnovich
Department of Chemistry
Harvard University
Cambridge, MA
telephone: 617-495-4130
facsimile: 617-496-5948
e-mail: eugene@onyx.harvard.edu

Research interests: Since 1982 Dr. Shaknovich's research interests were focused on understanding, on physical grounds, the mechanism of biological structure formation in relation to molecular evolution. One of the areas of great interest to him and his colleagues in the lab is theory of protein folding - understanding basic principles how proteins resolve the Levinthal paradox as well as building on that to develop new techniques for protein structure prediction. Other areas of active research interests include rational drug design, protein evolution/design, synthetic polymeric materials as biomimetics, the morphology and dynamics of complex polymer systems (gels, block-copolymers etc) studies in pattern recognition upon poilymer adsorption and viral inhibition.

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