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Physics Approach to Simplifying Complexity in Biology (6117)

December 15, 2014 – December 19, 2014

Location: Hong Kong, China

Organizers
Robert Austin, Princeton University
Henry Tye, Hong Kong University of Science and Technology
Lei-han Tang, Hong Kong Baptist University

Overview

The fundamental questions we will pose at this workshop are connected to the importance of functional protein conformational states and the gateway of emergent behavior between large proteins and chaperones in forming a functional proteome.

(A) Can large proteins really fold? That is, while they no doubt can collapse from the molten globule into some sort of three-dimensional distribution of conformational states, can they truly find the functional subset of the conformational distribution on a biologically relevant timescale “de novo”?
(B) To what extent do chaperone proteins guide “generically folded” proteins into biological active conformations? Are chaperones absolutely essential, and who then folds the chaperone proteins?
(C) How can we experimentally characterize the functional state of the proteome, the landscape of generically folded, functionally folded, and aggregated proteins?
(D) How is the emergent complexity of the functional proteome connected to the diseased state of the organism?

The venue will be the Institute for Advanced Studies (IAS) at the Hong Kong University of Science and Technology (HKUST) and ICAM branch. I am a Visiting Member of the IAS. The IAS is housed in an absolutely spectacular new building at the HKUST with state of the art meeting space.


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