Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM021900-09S1
Application #
3270787
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1978-09-01
Project End
1985-03-31
Budget Start
1984-04-01
Budget End
1985-03-31
Support Year
9
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Chicago
Department
Type
Schools of Medicine
DUNS #
225410919
City
Chicago
State
IL
Country
United States
Zip Code
60637

  Publications

Mustafi, D; Sosa-Peinado, A; Makinen, M W (2001) ENDOR structural characterization of a catalytically competent acylenzyme reaction intermediate of wild-type TEM-1 beta-lactamase confirms glutamate-166 as the base catalyst. Biochemistry 40:2397-409
Atanasov, B P; Mustafi, D; Makinen, M W (2000) Protonation of the beta-lactam nitrogen is the trigger event in the catalytic action of class A beta-lactamases. Proc Natl Acad Sci U S A 97:3160-5
Sosa-Peinado, A; Mustafi, D; Makinen, M W (2000) Overexpression and biosynthetic deuterium enrichment of TEM-1 beta-lactamase for structural characterization by magnetic resonance methods. Protein Expr Purif 19:235-45
Horvath, M P; Copeland, R A; Makinen, M W (1999) The second derivative electronic absorption spectrum of cytochrome c oxidase in the Soret region. Biophys J 77:1694-711
Makinen, M W (1998) Electron nuclear double resonance determined structures of enzyme reaction intermediates: structural evidence for substrate destabilization. Spectrochim Acta A Mol Biomol Spectrosc 54A:2269-81
Makinen, M W; Mustafi, D (1995) The vanadyl ion: molecular structure of coordinating ligands by electron paramagnetic resonance and electron nuclear double resonance spectroscopy. Met Ions Biol Syst 31:89-127
Mustafi, D; Nakagawa, Y (1994) Characterization of calcium-binding sites in the kidney stone inhibitor glycoprotein nephrocalcin with vanadyl ions: electron paramagnetic resonance and electron nuclear double resonance spectroscopy. Proc Natl Acad Sci U S A 91:11323-7
Mustafi, D; Makinen, M W (1994) Catalytic conformation of carboxypeptidase A. Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance. J Biol Chem 269:4587-95
Wells, G B; Mustafi, D; Makinen, M W (1994) Structure at the active site of an acylenzyme of alpha-chymotrypsin and implications for the catalytic mechanism. An electron nuclear double resonance study. J Biol Chem 269:4577-86
Makinen, M W; Troyer, J M; van der Werff, H et al. (1989) Dynamical structure of carboxypeptidase A. J Mol Biol 207:201-16

Showing the most recent 10 out of 12 publications