User:Sehat: Difference between revisions
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===Contact Info=== | ===Contact Info=== | ||
Sehat Nauli | '''Sehat Nauli''' | ||
UCLA Institute of Genomics and Proteomics | UCLA Institute of Genomics and Proteomics | ||
| Line 21: | Line 21: | ||
===Research Interests=== | ===Research Interests=== | ||
# Protein and | # Protein Design and Crystallization Modules | ||
# Membrane Protein Structures and Mechanism | # Membrane Protein Structures and Mechanism | ||
# Chemical Biology | # Chemical Biology | ||
===Publications=== | |||
*'''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''' | |||
Latest revision as of 10:55, 8 June 2006
Contact Info
Sehat Nauli
UCLA Institute of Genomics and Proteomics
Bowie Lab
Boyer Hall
611 Charles E Young East
Los Angeles, CA 90095
Email: sehat@ucla.edu
Bowie Lab at UC Los Angeles
Education
- 2003, PhD Biochemistry, University of Washington, Seattle
- 1998, BS Biochemistry, University of California, Los Angeles
Research Interests
- Protein Design and Crystallization Modules
- Membrane Protein Structures and Mechanism
- Chemical Biology
Publications
- 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
