The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Studies aimed at correlating structure and function, and experiments aimed at investigating protein folding are conducted. Structural studies for several proteins have been carried out. These comprise HIV-1 protease, cyanovirin-N,ubiquitin and a replication initiator protein. In addition, work was also carried out on different quaternary states of the model protein GB1 and on folding intermediates. New experiments were devised for measuring residual dipolar couplings.

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Intramural Research (Z01)
Project #
1Z01DK029025-15
Application #
6983742
Study Section
(LCP)
Project Start
Project End
Budget Start
Budget End
Support Year
15
Fiscal Year
2004
Total Cost
Indirect Cost
Name
U.S. National Inst Diabetes/Digst/Kidney
Department
Type
DUNS #
City
State
Country
United States
Zip Code
Louis, John M; Byeon, In-Ja L; Baxa, Ulrich et al. (2005) The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interface. J Mol Biol 348:687-98
Ding, Keyang; Gronenborn, Angela M (2004) Sensitivity-enhanced IPAP experiments for measuring one-bond 13C'-13Calpha and 13Calpha-1Halpha residual dipolar couplings in proteins. J Magn Reson 167:253-8
Ding, Keyang; Gronenborn, Angela M (2004) Protein Backbone 1H(N)-13Calpha and 15N-13Calpha residual dipolar and J couplings: new constraints for NMR structure determination. J Am Chem Soc 126:6232-3
Dangi, Bindi; Gronenborn, Angela M; Rosner, Judah L et al. (2004) Versatility of the carboxy-terminal domain of the alpha subunit of RNA polymerase in transcriptional activation: use of the DNA contact site as a protein contact site for MarA. Mol Microbiol 54:45-59
Ding, Keyang; Louis, John M; Gronenborn, Angela M (2004) Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR. J Mol Biol 335:1299-307
Byeon, In-Ja L; Louis, John M; Gronenborn, Angela M (2004) A captured folding intermediate involved in dimerization and domain-swapping of GB1. J Mol Biol 340:615-25
Mesleh, M F; Valentine, K G; Opella, S J et al. (2003) Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies. J Biomol NMR 25:55-61
Ishima, Rieko; Torchia, Dennis A; Lynch, Shannon M et al. (2003) Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. J Biol Chem 278:43311-9
Louis, John M; Ishima, Rieko; Nesheiwat, Issa et al. (2003) Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties. J Biol Chem 278:6085-92
Katoh, Etsuko; Louis, John M; Yamazaki, Toshimasa et al. (2003) A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex. Protein Sci 12:1376-85

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