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Title: Single-Molecule Study of Protein-Protein Interaction Dynamics in a Cell Signaling System

Journal Article · · Journal of Physical Chemistry B, 108(2):737-744
DOI:https://doi.org/10.1021/jp0306491· OSTI ID:15010574

We report a combined single-molecule fluorescence and molecular dynamics (MD) simulation study of protein-protein interactions in a GTP-binding intracellular signaling protein Cdc42 in complex with a downstream effector protein WASP. A 13- kDa WASP fragment which binds only the activated GTP-loaded Cdc42 was labeled with a novel solvatochromic dye and used to probe hydrophobic interactions significant to Cdc42/WASP recognition. Our single-molecule fluorescence measurements have shown conformational fluctuations of the protein complex and suggested multiple conformational states at a wide range of time scales might be involved in protein interaction dynamics. Single-molecule experiments have revealed the dynamic disorder or protein-protein interactions within the Cdc42/WASP complex, which may be important for regulating downstream signaling events.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
15010574
Report Number(s):
PNNL-SA-38567; 2179; 2462; 3277
Journal Information:
Journal of Physical Chemistry B, 108(2):737-744, Journal Name: Journal of Physical Chemistry B, 108(2):737-744
Country of Publication:
United States
Language:
English

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