Medicine and Health Sciences Commons^™

Structural And Dynamical Order Of A Disordered Protein: Molecular Insights Into Conformational Switching Of Page4 At The Systems Level, Xingcheng Lin, Prakash Kulkarni, Federico Bocci, Nicholas P. Schafer, Susmita Roy, Min-Yeh Tsai, Yanan He, Yihong Chen, Krithika Rajagopalan, Steven M. Mooney, Yu Zeng, Keith Weninger, Alex Grishaev, José N. Onuchic, Herbet Levine, Peter G. Wolynes, Ravi Salgia, Govindan Rangarajan, Vladimir N. Uversky, John Orban, Mohit Kumar Jolly

Molecular Medicine Faculty Publications

Folded proteins show a high degree of structural order and undergo (fairly constrained) collective motions related to their functions. On the other hand, intrinsically disordered proteins (IDPs), while lacking a well-defined three-dimensional structure, do exhibit some structural and dynamical ordering, but are less constrained in their motions than folded proteins. The larger structural plasticity of IDPs emphasizes the importance of entropically driven motions. Many IDPs undergo function-related disorder-to-order transitions driven by their interaction with specific binding partners. As experimental techniques become more sensitive and become better integrated with computational simulations, we are beginning to see how the modest structural ordering …