Many biological processes are carried out through the formation of macromolecular complexes, ranging from the simplest conformational organization to the most sophisticated interactions among complexes themselves. Reversible associations generate specific local conformations, active site configurations, and subunit - subunit interfaces, and encompass larger scale quaternary rearrangements and dissociation events. Assembled complexes exhibit properties different from those of component parts, such that "the whole is greater than the sum of the parts", resulting in biological functioning of the assembly.

This Gordon Research Conference brings together researchers from what may appear to be disparate fields with the common focus of applying quantitative kinetic and thermodynamic analysis to reversible macromolecular interactions. This conference will include the following session topics:

• Protein design in evolution and recognition
• Emerging technologies
• Single molecule mechanics
• Nucleic acid/protein recognition
• Lipid/protein recognition
• Protein switches and networks
• Advances in classic technologies
• Ligand/macromolecule complexes and drug design
• Selected student oral presentations

all from the perspective of reversibly associating systems. A wide array of techniques are typically covered, from single molecule to computational methods, chromatography and analytical ultracentrifugation, spectroscopic dynamics and titration calorimetry. The quantitative analysis of assembled complexes demonstrates that these biologically important functions depend not just upon a single part of the molecule, but on the coordination brought about by the ensemble of interactions.

Applications from graduate students and young postdoctoral scientists are welcomed. A selection of short talks will be invited from students presenting posters.