Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM052421-02
Application #
2191438
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1995-05-01
Project End
1999-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Physiology
Type
Organized Research Units
DUNS #
791277940
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Yip, Grover N B; Zuiderweg, Erik R P (2004) A phase cycle scheme that significantly suppresses offset-dependent artifacts in the R2-CPMG 15N relaxation experiment. J Magn Reson 171:25-36
Cai, Sheng; Stevens, Shawn Y; Budor, Andrew P et al. (2003) Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments. Biochemistry 42:11100-8
Hinton, Ayana; Zuiderweg, Erik R P; Ackerman, Sharon H (2003) A purified subfragment of yeast Atp11p retains full molecular chaperone activity. J Biol Chem 278:34110-3
Kern, Dorothee; Zuiderweg, Erik R P (2003) The role of dynamics in allosteric regulation. Curr Opin Struct Biol 13:748-57
Shao, Weiping; Im, Sang-Choul; Zuiderweg, Erik R P et al. (2003) Mapping the binding interface of the cytochrome b5-cytochrome c complex by nuclear magnetic resonance. Biochemistry 42:14774-84
Stevens, Shawn Y; Cai, Sheng; Pellecchia, Maurizio et al. (2003) The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG. Protein Sci 12:2588-96
Chung, Duane A; Zuiderweg, Erik R P; Fowler, Carol B et al. (2002) NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry 41:3596-604
Zuiderweg, Erik R P (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41:1-7
Khandelwal, P; Keliikuli, K; Smit, C L et al. (2001) 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide. J Biomol NMR 21:69-70
Hall, D A; Vander Kooi, C W; Stasik, C N et al. (2001) Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase. Proc Natl Acad Sci U S A 98:9521-6

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