Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
2R37DK017335-17
Application #
3483192
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1977-07-01
Project End
1994-12-31
Budget Start
1990-02-20
Budget End
1990-12-31
Support Year
17
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Wesleyan University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Middletown
State
CT
Country
United States
Zip Code
06459
LiCata, V J; Burz, D S; Moerke, N J et al. (1998) The magnitude of the allosteric conformational transition of aspartate transcarbamylase is altered by mutations. Biochemistry 37:17381-5
Hariharan, M; Allewell, N M (1998) Effects of the T-->R transition on the electrostatic properties of E. coli aspartate transcarbamylase. Proteins 32:200-10
LiCata, V J; Allewell, N M (1998) Solvent perturbation of the allosteric regulation of aspartate transcarbamylase. Biochim Biophys Acta 1384:306-14
Ha, Y; Allewell, N M (1998) Intersubunit hydrogen bond acts as a global molecular switch in Escherichia coli aspartate transcarbamoylase. Proteins 33:430-43
LiCata, V J; Allewell, N M (1997) Functionally linked hydration changes in Escherichia coli aspartate transcarbamylase and its catalytic subunit. Biochemistry 36:10161-7
Morizono, H; Listrom, C D; Rajagopal, B S et al. (1997) 'Late onset' ornithine transcarbamylase deficiency: function of three purified recombinant mutant enzymes. Hum Mol Genet 6:963-8
LiCata, V J; Allewell, N M (1997) Is substrate inhibition a consequence of allostery in aspartate transcarbamylase? Biophys Chem 64:225-34
Morizono, H; Tuchman, M; Rajagopal, B S et al. (1997) Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia. Biochem J 322 ( Pt 2):625-31
Oberoi, H; Trikha, J; Yuan, X et al. (1996) Identification and analysis of long-range electrostatic effects in proteins by computer modeling:aspartate transcarbamylase. Proteins 25:300-14
Yuan, X; LiCata, V J; Allewell, N M (1996) Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase. J Biol Chem 271:1285-94

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