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(Research Interests)
Current revision (13:55, 8 June 2006) (view source)
(Contact Info)
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===Contact Info===
===Contact Info===
Sehat Nauli
'''Sehat Nauli'''
UCLA Institute of Genomics and Proteomics
UCLA Institute of Genomics and Proteomics

Current revision


Contact Info

Sehat Nauli

UCLA Institute of Genomics and Proteomics

Bowie Lab

Boyer Hall

611 Charles E Young East

Los Angeles, CA 90095


Bowie Lab at UC Los Angeles


  • 2003, PhD Biochemistry, University of Washington, Seattle
  • 1998, BS Biochemistry, University of California, Los Angeles

Research Interests

  1. Protein Design and Crystallization Modules
  2. Membrane Protein Structures and Mechanism
  3. Chemical Biology


  • Nauli S, Kuhlman B, Le Trong I, Stenkamp RE, Teller D, Baker D. Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2. Protein Sci., 11(12):2924-31 PMID 12441390
  • Krantz BA, Srivastava AK, Nauli S, Baker D, Sauer RT, Sosnick TR. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects. Nat Struct Biol. 9(6):458-63 PMID 11979278
  • Nauli S, Kuhlman B, Baker D. Computer-based redesign of a protein folding pathway. Nat Struct Biol. 8(7):602-5 PMID 11427890
  • Zhou Y, Lau FW, Nauli S, Yang D, Bowie JU. Inactivation mechanism of the membrane protein diacylglycerol kinase in detergent solution. Protein Sci 10(2):378-83 PMID 11266623
  • Gu H, Doshi N, Kim DE, Simons KT, Santiago JV, Nauli S, Baker D. Robustness of protein folding kinetics to surface hydrophobic substitutions. Protein Sci 8(12):2734-41 PMID 10631990
  • Scalley ML, Nauli S, Gladwin ST, Baker D. Structural transitions in the protein L denatured state ensemble. Biochemistry 38(48):15927-35 PMID 10625459
  • Lau FW, Nauli S, Zhou Y, Bowie JU. Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation. J Mol Biol 290(2):559-64 PMID 10390353
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