Abstract

This research will develop organic syntheses and synthetic techniques based on enzymes as catalysts. It will emphasize: 1) Cofacyor regeneration (ATP, GTP, UTP, CTP, NAD, NADH, NADP, NADPH) 2) Syntheses of sugars and sugar derivatives (NAD, analogs of NAD and ATP, phosphoribosyl pyrophosphate, nucleoside diphosphate sugars, intermediates in glycolysis) 3) Synthetic techniques (chiral syntheses, protective group chemistry, reactions based on catalysis by aldolases, nucleoside phosphorylase, and cyclohexanone lactonase. 4) Protein stabilization (especially using gel immobilization)

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM030367-04
Application #
3278091
Study Section
Bio-Organic and Natural Products Chemistry Study Section (BNP)
Project Start
1982-04-01
Project End
1986-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
4
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Harvard University
Department
Type
Schools of Arts and Sciences
DUNS #
071723621
City
Cambridge
State
MA
Country
United States
Zip Code

  Publications

Mack, Eric T; Snyder, Phillip W; Perez-Castillejos, Raquel et al. (2012) Dependence of avidity on linker length for a bivalent ligand-bivalent receptor model system. J Am Chem Soc 134:333-45
Mirica, Katherine A; Lockett, Matthew R; Snyder, Phillip W et al. (2012) Selective precipitation and purification of monovalent proteins using oligovalent ligands and ammonium sulfate. Bioconjug Chem 23:293-9
Mecinovic, Jasmin; Snyder, Phillip W; Mirica, Katherine A et al. (2011) Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the ""hydrophobic wall"" of carbonic anhydrase. J Am Chem Soc 133:14017-26
Snyder, Phillip W; Mecinovic, Jasmin; Moustakas, Demetri T et al. (2011) Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase. Proc Natl Acad Sci U S A 108:17889-94
Mack, Eric T; Snyder, Phillip W; Perez-Castillejos, Raquel et al. (2011) Using covalent dimers of human carbonic anhydrase II to model bivalency in immunoglobulins. J Am Chem Soc 133:11701-15
Bilgiçer, Ba?ar; Thomas 3rd, Samuel W; Shaw, Bryan F et al. (2009) A non-chromatographic method for the purification of a bivalently active monoclonal IgG antibody from biological fluids. J Am Chem Soc 131:9361-7
Krishnamurthy, Vijay M; Kaufman, George K; Urbach, Adam R et al. (2008) Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding. Chem Rev 108:946-1051
Mack, Eric T; Perez-Castillejos, Raquel; Suo, Zhigang et al. (2008) Exact analysis of ligand-induced dimerization of monomeric receptors. Anal Chem 80:5550-5
Bilgicer, Basar; Moustakas, Demetri T; Whitesides, George M (2007) A synthetic trivalent hapten that aggregates anti-2,4-DNP IgG into bicyclic trimers. J Am Chem Soc 129:3722-8
Krishnamurthy, Vijay M; Semetey, Vincent; Bracher, Paul J et al. (2007) Dependence of effective molarity on linker length for an intramolecular protein-ligand system. J Am Chem Soc 129:1312-20

Showing the most recent 10 out of 67 publications