Institute for Protein Design

Neil King, PhD

Translational Investigator

Neil joined the Institute for Protein Design as a Translational Investigator in early 2014. During his postdoc, he pioneered the development of general computational methods for designing self-assembling proteins with atomic-level accuracy. His group at the IPD is using and extending these methods to design functional protein nanomaterials for applications in targeted drug delivery and the design of next-generation vaccines. Proteins are Nature’s building block of choice for the construction of ‘molecular machines’: stable yet dynamic assemblies with unparalleled abilities in molecular recognition, catalysis, and responsiveness to changes in environment. Neil’s group is incorporating these features into the design of functional nanomaterials with the goal of creating new opportunities for the treatment of disease. Working with collaborators at UW and the Fred Hutchinson Cancer Research Center, they are establishing a design-build-test cycle to use feedback from functional assays in vitro and in vivo to optimize the performance of the designed materials.

Neil P. King, PhD
Translational Investigator
Institute for Protein Design
University of Washington
J-Wing Health Sciences Building, Box 357370
Seattle, WA 98195-7370
Phone: 206-685-5082

Publications | Google Scholar Profile

[1] Neil P King, Jacob B Bale, William Sheffler, Dan E McNamara, Shane Gonen,Tamir Gonen, Todd O Yeates, David Baker (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature 510:103–108.

[2] Neil P King, Yen-Ting Lai (2013) Practical approaches to designing novel protein assemblies. Curr. Opin. Struct. Biol. 23:632–638.

[3] Yen-Ting Lai, Neil P King, Todd O Yeates (2012) Principles for designing ordered protein assemblies. Trends in Cell Biol. 22:653–661.

[4] Neil P King, William Sheffler, Michael R Sawaya, Breanna S Vollmar, John P Sumida, Ingemar André, Tamir Gonen, Todd O Yeates, David Baker (2012) Computational design of self-assembling protein nanomaterials with atomic level accuracy. Science 336:1171–1174.

• Press coverage by: NatureChemical & Engineering NewsBioWorldChemistry WorldBioTechniquesSpektrumUCLA

[5] Toby C Sayre, Toni M Lee, Neil P King, Todd O Yeates (2011) Protein stabilization in a highly knotted protein polymer. Protein Eng. Des. Sel. 24:627–630.

[6] Neil P King, Alex W Jacobitz, Michael R Sawaya, Lukasz Goldschmidt, Todd O Yeates (2010) Structure and folding of a designed knotted protein. Proc. Natl. Acad. Sci. U.S.A. 107:20732–20737.

• Commentary by: Shakhnovich E (2011) To knot or not to knot? Nat. Mater. 10:84–86.

[7] Neil P King, Toni M Lee, Michael R Sawaya, Duilio Cascio, Todd O Yeates (2008) Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon. J. Mol. Biol. 380:181–192.

[8] Todd O Yeates, Todd S Norcross, Neil P King (2007) Knotted and topologically complex proteins as models for studying folding and stability. Curr. Opin. Chem. Biol. 11:595–603.

[9] Neil P King, Eric O Yeates, Todd O Yeates (2007) Identification of rare slipknots in proteins and their implications for stability and folding. J. Mol. Biol. 373:153–166.