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 'unfolded' proteins often carry out important biological functions.

Disordered regions of sequence in some cases function to mechanically uncouple structured domains making their dyanmics less constrained: such linkers are important in a diverse collection of proteins, from viral attachment proteins to transcription factors. Disordered regions provide access for protease digestion: such directed digestion is apparently critical for the regulation of many important cellular processes.

Disorder-to-order transitions may be one of the major factors in biomechanics, for example in the development of force by protein assemblies. Finally, disordered regions are clearly involved in molecular recognition via disorder-to-order transitions: numerous examples of disorder-to-order upon complex formation are by now well-characterized, and biological advantages for this type of molecular recognition have been proposed.
 

Purpose of the Session

We hope to bring together an array of researchers who focus on different aspects of disordered or unfolded sequences. Although the Pacific Symposium on Biocomputing (PSB) has an overall computational emphasis, experimentalists and theorists are strongly encouraged to participate in the various scientific sessions.

 
Areas of Interest

If you are working on, or interested in, any aspect of disordered or unfolded sequences, we would like to invite you to participate in our session. Specifically, we seek manuscript submissions on the characterization and investigation of disordered or unfolded sequences using any approach whatsoever, but especially involving the following categories:

• Biophysical methods, such as NMR, hydrogen exchange, esr, x-ray diffraction, CD, fluorescence, optical tweezers, etc.;

• Biochemical methods, such as proteolysis, site directed mutagenensis, size exclusion chromatography, functional assays, etc.;

• Theoretical and computational methods, such as estimating foldability from lattice models, prediction of disorder from sequence, prediction of functional advantages for disordered regions from first principles, etc;

• In vivo methods, primarily regarding the dependence of targeted proteolysis on disordered regions of sequence.

Please respond to any of the co-chairs of this session by e-mail as soon as possible if you would like to participate in Disorder in Protein Structure and Function.
 

Session Co-chairs

A. Keith Dunker -
Department of Biochemistry,
Washington State University,
Pullman, WA 99164-4660
dunker@mail.wsu.edu

Charles Kissinger
Agouron Pharmaceuticals, Inc.
3565 General Atomics Court
San Diego, CA 92121
crk@agouron.com

Eugene Shakhnovich
Department of Chemistry
Harvard University
Cambridge, MA
eugene@onyx.harvard.edu