Melisenda Jean McDonald

Melisenda J. McDonald

Professor Emeritus

College
College of Sciences
Department
Chemistry
Email
Melisenda_McDonald@uml.edu

Expertise

Biochemistry

Research Interests

Biochemistry

Protein structure, function and assembly; hemoglobin; self-assembled protein systems; structural biology; immunobiochemistry; biosensor technology; self-mediated biosystems.

Education

  • Ph D: Biochemistry, (1973), State University of New York - Buffalo, New York
  • Ph D: Biochemistry, (1973), State University of New York - Buffalo, NY
  • MA: Biochemistry, (1971), State University of New York - Buffalo, New York
  • MA: Biochemistry, (1971), State University of New York - Buffalo, NY
  • BA: Biology/Chemistry, (1967), Dowling College - Oakdale, NY
  • BA: Biology/Chemistry, (1967), Dowling College - Oakdale, New York

Selected Awards and Honors

  • Editorial Board Member: Current Protein and Peptide Science - The Open Biochemistry Journal
  • Excellence in Teaching Award in Chemistry, Teaching - University of Massachusetts Lowell
  • Research Career Development Award - National Institutes of Health
  • Excellence in Teaching Award (2009) - UML
  • Editorial Board Member: The Open Biochemistry Journal (2007)
  • Editorial Board Member: Current Protein and Peptide Science (2004)
  • Excellence in Teaching Award (2004) - UML
  • Sigma Xi (2001)
  • Research Career Development Award (1982) - National Heart, Lung and Blood Institute, National Institutes of Health

Selected Publications

  • Farris, L.R., McDonald, M.J. (2012). Computational analysis of non-covalent polymer-protein interactions governing antibody orientation. Analytical and Bioanalytical Chemistry, 402(4) 1731-1736.
  • Patil, S., Chaudhury, P., Clarizia, L., McDonald, M.J., Reynaud, E., Gaines, P., Schmidt, D.F. (2012). Responsive hydrogels produced via organic sol-gel chemistry for cell culture applications. Acta Biomaterialia, 8(8) 2919-2931.
  • Farris, L.R., McDonald, M.J. (2011). AFM imaging of ALYGNSA polymer-protein surfaces: Evidence of antibody orientation. Analytical and Bioanalytical Chemistry, 401(9) 2821-2829.
  • Chourb, S., Mackness, B.C., Farris, L.R., McDonald, M.J. (2011). Improved detection of the MUC1 cancer antigen CA 15-3 by ALYGNSA fluorimmunoassay. Health, 3(8) 524-528.
  • Patil, S., Clarizia, L.J., McDonald, M.J., Reynaud, E., Schmidt, D.F. (2011). Responsive hydrogels produced via organic sol-gel chemistry for biomedical applications. Annual Technical Conference - Society of Plastics Engineers, 69th 2012-2016.
  • Farris, L.R., Wu, N., Wang, W., Clarizia, L.J., Wang, X., McDonald, M.J. (2010). Immuno-interferometric sensor for the detection of influenza A nucleoprotein. Analytical and Bioanalytical Chemistry, 396(2) 667-674.
  • Wu, N., Wang, W., Ling, Y., Farris, L., Kim, B., McDonald, M.J., Wang, X. (2010). Label-free detection of biomolecules using LED technology. Proceedings of SPIE, 7574 75740-75740.
  • MacKness, B.C., Chourb, S., Farris, L.R., McDonald, M.J. (2010). Polymer-protein-enhanced fluoroimmunoassay for prostate-specific antigen. Analytical and Bioanalytical Chemistry, 396(2) 681-686.
  • MacKness, B.C., McDonald, M.J. (2010). Serum-based ALYGNSA immunoassay for the prostate cancer biomarker, total prostate-specific antigen (tPSA). Analytical and Bioanalytical Chemistry, 397(7) 3151-3154.
  • Ling, Y., Wu, N., Wang, W., Farris, L.R., Kim, B., Wang, X., McDonald, M.J. (2010). Thin Film Thickness Variation Measurement Using Dual LEDs and Reflectometric Interference Spectroscopy Model in Biosensor SPIE Photonics West BiOS Exhibition: Optical Fibers and Sensors Optical Fibers and Sensors for Medical Diagnostics and Treatment Applications;. Proceedings of SPIE 75590K.
  • Clarizia, L.A., Sok, D., Wei, M., Mead, J., Barry, C., McDonald, M.J. (2009). Antibody orientation enhanced by selective polymer-protein noncovalent interactions. Analytical and bioanalytical chemistry, 393(5) 1531-8.
  • Chourb, S., Mackness, B.C., Farris, L.R., McDonald, M.J. (2009). Enhanced Immuno-Detection of Shed Extracellular Domain of HER-2/neu;. HEALTH, 1 325-329.
  • Wu, N., Wang, W., Farris, L.R., McDonald, M.J., Wang, X. (2009). Label-free Detection of Biomolecules Using an Optical Biosensor. The Fifth International Workshop on Advanced Smart Material and Smart Structures Technology, 644-649.
  • Sok, D., Clarizia, L.J., Farris, L.R., McDonald, M.J. (2009). Novel fluoroimmunoassay for ovarian cancer biomarker CA-125. Analytical and Bioanalytical Chemistry, 393(5) 1521-1523.
  • Wang, W., Ma, X., Clarizia, L.J., Wang, X., McDonald, M.J. (2009). Optical Interferometric Biosensor with PMMA as Functional Layer. Materials Research Society Symposium Proceedings, 1133 0-3.
  • Fonseka, P.V., Vasudevan, G., Clarizia, L.J., McDonald, M.J. (2007). Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly. Protein Journal, 26(4) 257-263.
  • Vasudevan, G., McDonald, M.J. (2006). Soret spectral and bioinformatic approaches provide evidence for a critical role of the -subunit in assembly of tetrameric hemoglobin. Protein Journal, 25(1) 45-56.
  • Claypool, K., Vasudevan, G., McDonald, M.J. (2004). Promethea: Building an integrated community of protein resources on the Web. Faseb Journal, 18(8).
  • Vasudevan, G., Fonseka, P., McDonald, M.J. (2004). Temperature dependent Soret spectral changes accompany CNHemin binding to apohemoglobin. Faseb Journal, 18(8).
  • Morris, A., McDonald, M.J. (2002). Carboxyl-terminal modification alters the subunit interactions and assembly pathways of normal and sickle hemoglobins. Journal of protein chemistry, 20(8) 611-617.
  • Jennings, T.M., McDonald, M.J. (2002). Esterification of the propionate groups promotes / hemoglobin chain homogeneity of CN-hemin binding. Biochemical and biophysical research communications, 293(5) 1354-1357.
  • Vasudevan, G., McDonald, M.J. (2002). Ordered heme binding ensures the assembly of fully functional hemoglobin: A hypothesis. Current Protein and Peptide Science, 3(4) 461-466.
  • Morris, A., McDonald, M.J. (2001). Carboxyl-terminal modification alters the subunit interactions and assembly pathways of normal and sickle hemoglobins. Journal of protein chemistry, 20(8) 611-617.
  • Adachi, K., Yang, Y., Joshi, A.A., Vasudevan, G., Morris, A., McDonald, M.J. (2001). Consequence of 16 and 112 replacements on the kinetics of hemoglobin assembly. Biochemical and biophysical research communications, 289(1) 75-79.
  • McDonald, M.J., Morris, A., Vasudevan, G. (2000). Carboxyl-terminal modification alters the subunit interactions and assembly pathways of HbA and HbS. Faseb Journal, 14(8).
  • Chiu, F., Vasudevan, G., Morris, A., McDonald, M.J. (2000). Soret spectroscopic and molecular graphic analysis of human semi- -hemoglobin formation. Protein Journal, 19(2) 157-162.
  • Yamaguchi, T., Yang, Y., McDonald, M.J., Adachi, K. (2000). Surface and interface -chain residues synergistically affect hemoglobin assembly. Biochemical and biophysical research communications, 270(3) 683-687.
  • Vasudevan, G., McDonald, M.J. (2000). Wavelength-dependent spectral changes accompany CN-hemin binding to human apohemoglobin. Journal of protein chemistry, 19(7) 583-590.
  • Vasudevan, G., McDonald, M.J. (1998). Analysis of the global architecture of hemoglobin A2 by heme binding studies and molecular modeling. Protein Journal, 17(4) 319-327.
  • Chiu, F., Vasudevan, G., Morris, A., McDonald, M.J. (1998). Fluorescence studies of human semi- -hemoglobin assembly. Biochemical and biophysical research communications, 242(2) 365-368.
  • Vasudevan, G., McDonald, M.J. (1997). Spectral demonstration of semihemoglobin formation during CN-hemin incorporation into human apohemoglobins. Journal of Biological Chemistry, 272(1) 517-524.
  • Moulton, D.P., Morris, A., Vasudevan, G., Chiu, F.M., McDonald, M.J. (1996). Carboxyl-terminal modification influences subunit assembly of sickle hemoglobin beta chains. Biochemical and biophysical research communications, 226(2).
  • Moulton, D.P., Joshi, A.A., Morris, A., McDonald, M.J. (1994). Effect of Carboxyterminal Modification on the Oligomeric Structure of Human Beta-Hemoglobin. Biochemical and biophysical research communications, 204(2).
  • O'Malley, S.M., McDonald, M.J. (1994). Fluorescence studies of normal and sickle beta apohemoglobin self- association. Journal of protein chemistry, 13(7) 585-590.
  • Omalley, S.M., McDonald, M.J. (1994). Fluorescence Studies of Normal and Sickle Beta-Apohemoglobin Self-Association. Journal of protein chemistry, 13(7).
  • Moulton, D.P., McDonald, M.J. (1994). Kinetics of Human Apohemoglobin Dimer Dissociation. Biochemical and biophysical research communications, 199(3).
  • O'Malley, S.M., McDonald, M.J. (1994). Monitoring the effect of subunit assembly on the structural flexibility of human alpha apohemoglobin by steady-state fluorescence. Journal of protein chemistry, 13(6) 561-567.
  • Omalley, S.M., McDonald, M.J. (1994). Monitoring the Effect of Subunit Assembly on the Structural Flexibility of Human Alpha-Apohemoglobin by Steady-State Fluorescence. Journal of protein chemistry, 13(6).
  • Wei, Y.Z., Kumbharkhane, A.C., Sadeghi, M., Sage, J.T., Tian, W.D., Champion, P.M., Sridhar, S., McDonald, M.J. (1994). Protein hydration investigations with high-frequency dielectric spectroscopy. Journal of Physical Chemistry, 98(26) 6644-6651.
  • Joshi, A.A., McDonald, M.J. (1994). Role of and carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly. Journal of Biological Chemistry, 269(11) 8549-53.
  • Joshi, A.A., McDonald, M.J. (1994). Role of and carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly. Journal of Biological Chemistry, 269(11) 8549-8553.
  • Joshi, A.A., McDonald, M.J. (1994). Role of Alpha-Carboxyl-Terminal and Beta-Carboxyl-Terminal Residues in the Kinetics of Human Oxyhemoglobin Dimer Assembly. Journal of Biological Chemistry, 269(11).
  • O'Malley, S.M., McDonald, M.J. (1994). Steady state fluorescence energy transfer measurements of human alpha apohemoglobin structure. Biochemical and biophysical research communications, 200(1) 384-388.
  • Omalley, S.M., McDonald, M.J. (1994). Steady-State Fluorescence Energy-Transfer Measurements of Human Alpha-Apohemoglobin Structure. Biochemical and biophysical research communications, 200(1).
  • Moulton, D.P., McDonald, M.J. (1993). Rate of Dissociation of the Human Apohemoglobin Dimer. Biophysical journal, 64(2).
  • Moopenn, W.F., Hine, T.K., Johnson, M.H., Jue, D.L., Holland, S., George, S., Pierce, A.M., Michalski, L.A., McDonald, M.J. (1992). Hb Rancho Mirage [Beta-143(h21)his-]Asp] - a Variant in the 2,3-Dpg Binding-Site Showing Normal Oxygen-Affinity at Physiological Ph. Hemoglobin, 16(1-2).
  • Omalley, S.M., McDonald, M.J. (1992). Intrinsic Tryptophanyl Fluorescence Properties of Human Normal and Sickle Beta Apohemoglobin are Concentration Dependent. Faseb Journal, 6(1).
  • Joshi, A.A., McDonald, M.J. (1992). The Effect of Carboxyterminal Modification on the Kinetics of Human Oxyhemoglobin Assembly. Faseb Journal, 6(1).
  • McDonald, M.J., Michalski, L.A., Turci, S.M., Guillette, R.A., Jue, D.L., Johnson, M.H., Moo-Penn, W.F. (1990). Structural, functional, and subunit assembly properties of hemoglobin Attleboro [ 138 (H21) Ser Pro], a variant possessing a site mutation at a critical C-terminal residue. Biochemistry, 29(1) 173-178.
  • Omalley, S.M., McDonald, M.J. (1990). The Effect of Ph on the Structure of Alpha-Apohemoglobin Measured by Steady-State Fluorescence Energy-Transfer. Biophysical journal, 57(2).
  • Youl Park, R., McDonald, M.J. (1989). Kinetics of heme binding to semi-alpha-hemoglobin. Biochemical and biophysical research communications, 162(1) 522-527.
  • Park, R.Y., McDonald, M.J. (1989). Kinetics of Heme Binding to Semi-Alpha-Hemoglobin. Biochemical and biophysical research communications, 162(1).
  • Michalski, L.A., McDonald, M.J. (1988). An investigation of human oxyhemoglobin beta tetramer dissociation using haptoglobin binding. Biochemical and biophysical research communications, 156(1) 438-444.
  • McDonald, M.J., Turci, S.M., Michalski, L.A. (1988). The Kinetics of Human Oxyhemoglobin Reconstitution. Biophysical journal, 53(2).
  • McDonald, M.J., Michalski, L.A. (1987). Haptoglobin Induces a Change in the Visible Spectrum of Human Oxyhemoglobin Beta-Chains. Federation proceedings, 46(6).
  • McDonald, M.J., Turci, S.M., Mrabet, N.T., Himelstein, B.P., Bunn, H. (1987). The kinetics of assembly of normal and variant human oxyhemoglobins. J Biol Chem, 262 5951-5956.
  • Mrabet, N.T., Shaeffer, J.R., McDonald, M.J., Bunn, H.F. (1986). Dissociation of dimers of human hemoglobins A and F into monomers. J Biol Chem, 261 1111-1115.
  • Mrabet, N.T., McDonald, M.J., Turci, S.M., Sarker, R., Szabo, A., Bunn, H.F. (1986). Electrostatic attraction governs the dimer assembly of human hemoglobins. J Biol Chem, 261 5222-5228.
  • McDonald, M.J., Turci, S.M., Bleichman, M., Stinson, R.A. (1985). Functional and subunit assembly properties of Hemoglobin Alberta. J Mol Biol, 183 105-112.
  • Turci, S.M., McDonald, M.J. (1985). Isolation of normal and variant human hemoglobin subunits. J Chroma, 343 168-174.
  • Shaeffer, J.R., McDonald, M.J., Turci, S.M., Dinda, D.M., Bunn, H.F. (1984). Dimer-monomer dissociation of human hemoglobin. A.J Biol Chem, 259 14544-14547.
  • Moo-Penn, W.F., Jue, D.L., Johnson, M.H., McDonald, M.J., Turci, S.M., Shih, T.B., Jones, R.T., Therrell, B.L., Arnone, A. (1984). Structural and functional studies of HbA Wayne, an elongated chain variant. J Mol Biol, 180 1119-1140.
  • McDonald, M.J., Turci, S.M., Bunn, H.F., Brewer, G.J. (1984). Subunit assembly of normal and variant human hemoglobins. In: The Red Cell. Progress in Clin and Biol Res., 65 3-15.
  • Bunn, H.F., McDonald, M.J. (1983). Electrostatic interactions in the assembly of hemoglobin. Nature, 306 498-500.
  • Turci, S.M., McDonald, M.J. (1983). The effect of pH on the rate of dissociation of the oxygenated chain tetramer of HbA A. Biochem Biophys Res Com., 111 55-60.
  • Chiou, S.H., Garrick, L.M., McDonald, M.J. (1982). Functional properties of human adult hemoglobin specifically modified at the -amino groups of the chains with D-glucose-6-phosphate. Biochemistry, 21 13-20.
  • Bunn, H.F., McDonald, M.J., Shapiro, R., Ho, E. (1982). Modification of hemoglobin structure and function by nonenzymatic glycosylation. Hemoglobin and Oxygen binding. Elsevier North Holland, New York,, 301-305.
  • McDonald, M.J. (1981). Assembly of human adult and sickle hemoglobins from their oxygenated subunits. Differential rates of chain tetramer dissociation. J Biol Chem, 256 6487-6490.
  • Shaeffer, J.R., McDonald, M.J., Bunn, H.F. (1981). Assembly of normal and abnormal human hemoglobins. Trends in biochemical sciences, 6 158-161.
  • Bunn, H.F., McDonald, M.J., Shapiro, A., Cole, A., Brewer, G.J., Hanash, S.M. (1981). Chromatographic analysis of glycosylated hemoglobin. Advances in Hemoglobin Analysis. Progress in Clin and Biol Res., 60 83-94.
  • McDonald, M.J., Turci, S.M., Bunn, H.F., Garrick, L.M., Brewer, G.J. (1981). Hemoglobin structural and functional studies of genetically selected high and low level DPG rat strains. The Red Cell. Progress in Clin and Biol Res., 55 215-222.
  • McDonald, M.J., Shaeffer, J.R., Turci, S.M., Bunn, H.F., Brewer, G.J. (1981). Subunit assembly of hemoglobin A and S. In: The Red Cell. Progress in Clin and Biol Res., 55 27-36.
  • McDonald, M.J., Lund, D., Bleichman, M., Bunn, H.F., DeYoung, A., Noble, R.W., Foster, B., Arnone, A. (1980). Equilibrium, kinetic and structural properties of hemoglobin Cranston, a human variant with an elongated chain. J Mol Biol, 140 353-375.
  • Bunn, H.F., McDonald, M.J., Shapiro, R., Srivastave, S.K. (1980). Non-enzymatic glycosylation of hemoglobin and proteins of the erythrocyte membrane. In: Red Blood Cells and Lens Metabolism (pp. 455-462). Elsevier North Holland, Inc., New York,
  • Garrick, L.M., McDonald, M.J., Shapiro, R., Bleichman, M., McManus, M., Bunn, H.F. (1980). Structural analysis of the minor human hemoglobin components: HbA 1a1, HbA 1a2 and HbA 1b. Eur J Biochem, 106 353-359.
  • Solway, J., McDonald, M.J., Bunn, H.F., Aun, F., Cole, R., Soeldner, S. (1979). Biosynthesis of glycosylated hemoglobins in the monkey. J Lab Clin Med, 93 962-972.
  • McDonald, M.J., Bleichman, M., Bunn, H.F., Noble, R.W. (1979). Functional properties of the glycosylated minor components of human adult hemoglobin. J Biol Chem, 254 702-707.
  • Shapiro, R., McManus, M., Garrick, L., McDonald, M.J., Bunn, H.F. (1979). Non-enzymatic glycosylation of human hemoglobin at multiple sites. Metabolism, 28 427-430.
  • Bunn, H.F., Shapiro, R., McManus, M., Garrick, L., McDonald, M.J., Gallop, P.M., Gabbay, K.H. (1979). Structural heterogeneity of human hemoglobin A due to non-enzymatic glycosylation. Journal of Biological Chemistry, 254 3892-3898.
  • Shaeffer, J.R., Kingston, R.E., McDonald, M.J., Bunn, H.F. (1978). Competition of normal hemoglobin chains and sickle chains for chains as a post-translational control mechanism. Nature, 276 631-633.
  • McDonald, M.J., Shapiro, R., Bleichman, M., Solway, J., Bunn, H.F. (1978). Glycosylated minor components of human adult hemoglobin. Purification, identification and partial structural analysis. J Biol Chem, 253 2327-2332.
  • Bunn, H.F., McDonald, M.J., Caughey, W.S. (1978). Glycosylation of human hemoglobin. In: Biochemical and Clinical Aspects of Hemoglobin Abnormalities. Academic Press, New York,, 215-226.
  • McDonald, M.J., Tan-Wilson, A.L., Kosman, D.J., DeYoung, A., Noble, R.W. (1977). Ligand induced conformational changes in spin label modified human hemoglobins and chains and their carboxypeptidase A-digested derivatives. Biochem Biophys Acta. Biochem Biophys Acta., 490 51-61.
  • Bunn, H.F., Shapiro, R., McDonald, M.J., Haney, D.N. (1977). The interaction of glucose with hemoglobin. In: Molecular Interaction of Hemoglobin (pp. 299-308).
  • McDonald, M.J., Noble, R.W., Sharma, V.S., Ranney, H.M., Crookston, J.H., Schwartz, J.M. (1975). A comparison of the functional properties of two lepore hemoglobins with those of hemoglobin. A.J Mol Biol, 94 305-310.
  • McDonald, M.J., Ranney, H.M., Noble, R.W. (1975). Kinetics of ligand binding to ferrous heme groups of hemoglobin. M Saskatoon.J Mol Biol, 91 471-475.
  • Hoffman, B.M., Gibson, Q.H., Bull, C., Crepeau, R.H., Edelstein, S.J., Fisher, R.G., McDonald, M.J. (1975). Manganese-substituted hemoglobin and myoglobin. Ann NY Acad Sci, 224 174-186.
  • Garrick, L.M., Sharma, V.S., McDonald, M.J., Ranney, H.M. (1975). Rat hemoglobin heterogeneity: Two structurally distinct chains and functional behavior of selected components. The Biochemical journal, 149 245-258.
  • Salhany, J.M., Castillo, C.L., McDonald, M.J., Gibson, Q.H. (1975). The magnitude of subunit inequivalence for oxygen release from hemoglobin: A reinvestigation of the oxygen-pulse experiment. Proc Nat Acad Sci, 72 3998-4002.
  • Knowles, F.C., McDonald, M.J., Gibson, Q. (1975). The origin of the Adams-Schuster difference spectrum of oxyhemoglobin. Biochem Biophys Res Com, 66 556-563.
  • McDonald, M.J., Noble, R.W., Sharma, V.S., Ranney, H.M. (1974). Equilibrium and kinetic studies of hemoglobin I: A functionally silent amino acid substitution at an invariant residue. J Mol Biol, 89 245-248.
  • McDonald, M.J., Noble, R.W. (1974). Ligand dependent conformational changes in the isolated subunits and intact tetramers of human adult and fetal hemoglobins. J Biol Chem, 249 3161-3165.
  • McDonald, M.J., Noble, R.W. (1972). The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobins and their subunits. J Biol Chem, 247 4282-4287.
  • McDonald, M.J., Bahl, D.P. (1971). N-Acetylgalactosaminidase from Aspergillus niger. Methods in Enzymology. Complex Carbohydrates Part B, 28 754-738.

Selected Intellectual Property

  • Patent - Clarizia, L., Schmidt, D., Reynaud, E., McDonald, M., Wang, X."Cell culture hydrogel and pH detection system," 20090190135 United States
  • Patent - "Cell culture hydrogel and pH detection system," 61/004,560 United States
  • Patent - Clarizia, L., Mead, J., McDonald, M."Polymer-Protein Substrates for Immunosorbent Flourescence Assays," 60/874,807 United States
  • Patent - "Polymer-Protein Substrates for Immunosorbent Fluorescence Assays," 60/874,807 United States

Selected Contracts, Fellowships, Grants and Sponsored Research

  • A Plausible Model for Deoxy Hemoglobin (), - National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health
    McDonald, M. (Principal)
  • Subunit Assembly of Human Hemoglobins - Research Career Development Award (), Sponsored Research -
  • Conformational Requirements for the Polymerization of Sickle Hemoglobin (1979), Sponsored Research - The William F. Milton Fund of Harvard University
  • Conformational Requirements for the Polymerization of Sickle Hemoglobin (1979), Sponsored Research - The William F. Milton Fund of Harvard University
    McDonald, M. (Principal)
  • Nanomanufacturing of Multifunctional Sensors (2010), Contract -
    McDonald, M.J. (Principal)
  • Nanomanufacturing of Multifunctional Sensors (2007), - U.S. Army Research Office
    McDonald, M., Mead, J.
  • PI: Nanomanufacturing of Multifunctional Sensors" (2007), Grant - U.S. Army Research Office
  • Nanomanufacturing of Multifunctional Sensors (2009), -
    McDonald, M.J. (Principal)
  • Nanomanufacturing of Multifunctional Sensors (2007), Grant -
    McDonald, M.J. (Principal)
  • Cell culture hydrogel and pH detection system (2008), - UMASS CVIP
    McDonald, M. (Principal)
  • Cell culture hydrogel and pH detection system (2008), Grant - UMASS CVIP Award
  • NANI Technology Feasibility Study (2008), Grant -
    McDonald, M.J. (Principal)
  • Novel Hydrogel-Based System for Maintenance of Mammalian Cells in Culture (), - University of Massachusetts Commercial Ventures and Intellectual Property (CVIP) Technology Development Fund Award
    Schmidt, D., Reynaud, E., Reynaud, E., McDonald, M.J., Wang, X., Clarizia, L.
  • Novel Hydrogel-Based System for Maintenance of Mammalian Cells in Culture (Materials Transfer Agreement) (), -
    Schmidt, D., Wang, X., McDonald, M.J., Reynaud, E., Clarizia, L.
  • Polymer-Protein Substrates for Immunosorbent Flourescence Assays (2007), - UMASS CVIP
    McDonald, M. (Principal)
  • Polymer-Protein Substrates for Immunosorbent Fluorescence Assays (2007), Grant - UMASS CVIP Award
  • Novel Automated Nutrient Incorporation (NANI) System (), - Accelerated Technology Transfer Teams (AT³) Program, UML Nanomanufacturing Center of Excellence
    Schmidt, D., McDonald, M.J., Reynaud, E., Wang, X.
  • Intramolecular Chaperones of Human Hemoglobin Evaluated by Recominant Technology (2000), Grant - University of Massachusetts Lowell
    McDonald, M. (Co-Principal), Skare, I. (Co-Principal)
  • Intramolecular Chaperones of Human Hemoglobin Evaluated by Recombinant Technology (2000), Grant - UML Seed Grant
  • Subunit Assembly of Normal and Variant Hemoglobin (1986), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
  • Subunit Assembly of Normal and Variant Hemoglobins (1986), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
    McDonald, M. (Principal)
  • Subunit Assembly of Human Hemoglobins (1985), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
  • Subunit Assembly of Normal and Variant Hemoglobins (1985), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
    McDonald, M. (Principal)
  • Subunit Assembly of Human Hemoglobins (1982), Sponsored Research - National Heart, Lung and Blood Institute, National Institutes of Health
    McDonald, M. (Principal)
  • Subunit Assembly of Human Hemoglobins - Research Career Development Award (1982), Sponsored Research - National Heart, Lung and Blood Institute, National Institutes of Health
  • Subunit Assembly of Human Hemoglobins (1982), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
  • Subunit Assembly of Normal and Variant Hemoglobins (1982), Grant - National Heart, Lung and Blood Institute, National Institutes of Health
    McDonald, M. (Principal)
  • A Plausible Model for Deoxy Hemoglobin", Research Fellowship Awards (1974), Fellowship - National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health