1.
Our first aim i s to better understand the molecular basis of DNA-protein recognition and the regulation of gene expression. Specifically, we will continue studies of the cro repressor protein from bacteriophage lambda, for which we have recently determined the three-dimensional structure. We will attempt to determine the structure of cro complexed with appropriate DNA fragments. Also, we will attempt to determine the structures of the cII gene activator protein and single-strand DNA-binding proteins, as well as complexes of these proteins with DNA. 2. Our second goal is to better understand the factors that determine the structure, stability, dynamics, folding, activity and evolution of proteins. We believe that our ongoing structural and comparative studies of phage lysozyme, goose lysozyme, thermolysin and other proteins provide a very favorable experimental framework within which to address these problem areas.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM020066-16
Application #
3269883
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1979-01-01
Project End
1988-12-31
Budget Start
1988-01-01
Budget End
1988-12-31
Support Year
16
Fiscal Year
1988
Total Cost
Indirect Cost
Name
University of Oregon
Department
Type
Organized Research Units
DUNS #
948117312
City
Eugene
State
OR
Country
United States
Zip Code
97403
Juers, Douglas H; Rob, Beatrice; Dugdale, Megan L et al. (2009) Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli). Protein Sci 18:1281-92
Kingston, Richard L; Gay, Leslie S; Baase, Walter S et al. (2008) Structure of the nucleocapsid-binding domain from the mumps virus polymerase;an example of protein folding induced by crystallization. J Mol Biol 379:719-31
Busam, Robert D (2008) Structure of Escherichia coli exonuclease I in complex with thymidine 5'-monophosphate. Acta Crystallogr D Biol Crystallogr 64:206-10
Juers, Douglas H; Lovelace, Jeffrey; Bellamy, Henry D et al. (2007) Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing. Acta Crystallogr D Biol Crystallogr 63:1139-53
Tronrud, Dale E (2007) Introduction to macromolecular refinement. Methods Mol Biol 364:231-54
Wood, Zachary A; Weaver, Larry H; Brown, Patrick H et al. (2006) Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J Mol Biol 357:509-23
Addlagatta, Anthony; Quillin, Michael L; Omotoso, Omonike et al. (2005) Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry 44:7166-74
Ostheimer, Gerard J; Hadjivassiliou, Haralambos; Hadjivasiliou, Haralambos et al. (2005) Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. J Mol Biol 345:51-68
Juers, Douglas H; Kim, Jaeseung; Matthews, Brian W et al. (2005) Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin. Biochemistry 44:16524-8
Yousef, Mohammad S; Matthews, Brian W (2005) Structural basis of Prospero-DNA interaction: implications for transcription regulation in developing cells. Structure 13:601-7

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