Guo, Zhefeng


Associate Professor, Neurology

Member, Biochemistry, Biophysics & Structural Biology GPB Home Area

Brain Research Institute

Neuroscience GPB Home Area

Contact Information

Lab Number: 310-794-9503
Work Phone Number: 310-206-8773

Office Address:

4155 Reed



Zhefeng Guo is a structural biologist and biochemist who joined the UCLA School of Medicine faculty in 2008. Dr. Guo earned his B.S. in Microbiology (1995) at Shandong University and M.S. in Biochemistry (1998) at Peking University in China. Then Dr. Guo came to the United States for graduate studies and received his Ph.D. in Biochemistry (2003) at UCLA, where he was focused on developing electron paramagnetic resonance (EPR) methods to study protein structure, dynamics, and folding in Wayne Hubbell's laboratory. In 2004, Dr. Guo joined David Eisenberg's research group for postdoc training, working on the structural characterization of amyloid fibrils using the approaches of protein engineering and X-ray crystallography. His laboratory is currently investigating the structure and fibrillization mechanism of amyloid fibrils related to a wide range of human disorders such as Alzheimer's, Parkinson's and prion diseases, with the goal of developing molecular diagnostics and therapeutics for amyloid diseases


A selected list of publications:

Gu Lei, Tran Joyce, Jiang Lin, Guo Zhefeng   A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling Journal of structural biology, 2016; 194(1): 61-7.
Gu Lei, Liu Cong, Stroud James C, Ngo Sam, Jiang Lin & Guo Zhefeng   Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers Journal of Biological Chemistry, 2014; 10.1074/jbc.M114.569004.
Gu, Lei; Liu, Cong & Guo, Zhefeng   Structural insights into Aβ42 oligomers using site-directed spin labeling Journal of Biological Chemistry, 2013; 288: 18673-18683. Selected as JBC "Paper of the Week".
Gu, Lei & Guo, Zhefeng   Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils Journal of Neurochemistry, 2013; 126: 305-311.
Agopian, Audrey & Guo, Zhefeng   Structural origin of polymorphism of Alzheimer's amyloid β-fibrils Biochemical Journal, 2012; 447: 43-50.
Ngo, Sam; Chiang, Vicky; Ho, Elaine; Le, Linh & Guo, Zhefeng   Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study, PLoS ONE, 2012; 7: e47248.
Gu, Lei; Ngo, Sam & Guo, Zhefeng   Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments Journal of Biological Chemistry, 2012; 287: 9081-9.
Ngo, Sam & Guo, Zhefeng   Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease Biochemical and Biophysical Research Communications, 2011; 414: 512-6.
Ngo, Sam; Gu, Lei & Guo, Zhefeng   Hierarchical organization in the amyloid core of yeast prion protein Ure2 Journal of Biological Chemistry, 2011; 286: 29691-29699.
Lopez, Carlos J; Fleissner, Mark R; Guo, Zhefeng; Kusnetzow, Ana K & Hubbell, Wayne L   Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins Protein Science, 2009; 18: 1637-52.
Guo, Zhefeng; Cascio, Dulio; Hideg, Kalman & Hubbell, Wayne L.   Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme Protein Science, 2008; 17: 228-239.
Guo, Zhefeng & Eisenberg, David   The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold Protein Science, 2008; 17: 1617-1623.
Guo, Zhefeng & Eisenberg, David   The mechanism of the amyloidogenic conversion of T7 endonuclease I Journal of Biological Chemistry, 2007; 282: 14968-74.
Guo, Zhefeng; Cascio, Dulio; Hideg, Kalman; Kalai, Tamas & Hubbell, Wayne L.   Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme Protein Science, 2007; 16: 1069-1086.
Guo, Zhefeng & Eisenberg, David   Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I Proceedings of the National Academy of Sciences of USA, 2006; 103: 8042-7.