Abstract

NMR Spectroscopy will continue to be applied to determine the structure and dynamics of transfer RNA in interaction with the enzyme aminoacyl tRNA synthetase. These two macromolecules are essential parts of the biosynthetic machinery of all living things. The emphasis is on use of isotope labels of 15N and 13C to highlight proton NMR signals and provide more information than straight NMR spectroscopy. Smaller molecules interacting with the enzyme, as well as labelled enzyme and labelled tRNA, will be examined to provide information on molecular changes during function of the molecules. The NMR methods being used are prototypical of methods potentially applicable to drug design.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37GM020168-18
Application #
3484347
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1976-06-01
Project End
1991-07-31
Budget Start
1990-08-01
Budget End
1991-07-31
Support Year
18
Fiscal Year
1990
Total Cost
Indirect Cost

  Institution

Name
Brandeis University
Department
Type
Schools of Arts and Sciences
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454

  Publications

Halkides, C J; Farrar, C T; Singel, D J (1998) The effects of cryoprotection on the structure and activity of p21 ras: implications for electron spin-echo envelope modulation spectroscopy. J Magn Reson 134:142-53
Farrar, C T; Halkides, C J; Singel, D J (1997) The frozen solution structure of p21 ras determined by ESEEM spectroscopy reveals weak coordination of Thr35 to the active site metal ion. Structure 5:1055-66
Bellew, B F; Halkides, C J; Gerfen, G J et al. (1996) High frequency (139.5 GHz) electron paramagnetic resonance characterization of Mn(II)-H2(17)O interactions in GDP and GTP forms of p21 ras. Biochemistry 35:12186-93
Halkides, C J; Farrar, C T; Larsen, R G et al. (1994) Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms. Biochemistry 33:4019-35
Choi, B S; Redfield, A G (1992) NMR study of nitrogen-15-labeled Escherichia coli valine transfer RNA. Biochemistry 31:12799-802
Lowry, D F; Ahmadian, M R; Redfield, A G et al. (1992) NMR study of the phosphate-binding loops of Thermus thermophilus elongation factor Tu. Biochemistry 31:2977-82
Ye, X M; Pochapsky, T C; Pochapsky, S S (1992) 1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas. Biochemistry 31:1961-8
Miller, A F; Papastavros, M Z; Redfield, A G (1992) NMR studies of the conformational change in human N-p21ras produced by replacement of bound GDP with the GTP analog GTP gamma S. Biochemistry 31:10208-16
Pochapsky, T C; Ye, X M (1991) 1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin. Biochemistry 30:3850-6
Hall, K B; McLaughlin, L W (1991) Thermodynamic and structural properties of pentamer DNA.DNA, RNA.RNA, and DNA.RNA duplexes of identical sequence. Biochemistry 30:10606-13

Showing the most recent 10 out of 28 publications