Jane Dyson, PhD (Scripps)

"Functional roles of disorder and partial order in proteins"

When Jan 27, 2015
from 11:00 AM to 12:00 PM
Where Bioinformatics 1131
Contact Name
Attendees Open to the public
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Joint UNC Biochemistry & Biophysics and UNC Program in Molecular & Cellular Biophysics Seminar:

"Functional roles of disorder and partial order in proteins"

Jane Dyson

Jane Dyson, PhD

Department of Molecular Biology
Scripps Research Institute


Abstract: The eukaryotic proteome contains proteins that populate a wide variety of structural forms. Fully folded proteins are the most familiar from structural studies, but disordered and partly folded forms are also functional. Some proteins and protein domains are completely disordered, and this disorder is required for their correct function. Cellular signaling is one area where a number of functional disordered and partly ordered proteins play a part. We have been exploring the role of disorder in the interactions of the transcription factor NFκB with its inhibitor protein IκBα by measuring NMR spectra of component domains of these proteins. Disorder and partial order in IκBα contributes to the affinity and specificity of its interaction with NFκB, particularly in its competition for DNA-bound NFκB. Disorder and partial order are also observed in NFκB, adding to the complexity of its interactions with both IκBα and DNA. These studies illustrate the role of flexibility in the interactions of polypeptide chains as they interact to perform their functions.

Host: Nikolay Dokholyan, PhD