Email Muriel Maurer
Phone Number: (502) 852-7008 (Office)
Fax Number: (502) 852-8149
Address: Department of Chemistry
University of Louisville
Louisville, KY 40292
Ph. D. 1993, University of Virginia

Additional Appointments:

• Associate Professor, Department of Chemistry, University of Louisville, Louisville, KY (2003- )

Investigators:

• Madhavi A. Jadhav, Graduate Student
• Prakash G. Doiphode, Graduate Student
• Marina Malovichko, Graduate Student
• Ricky Woofter, Graduate Student
• Whitney Goldsberry, Undergraduate Student

Research Interests:

• Biochemistry: protein-structure function relationships, enzyme-ligand interactions

• Blood Coagulation: Factor XIII, Thrombin, Fibrinogen, Protease Activated Receptors

• Methods: enzyme kinetics, Nuclear Magnetic Resonance, MALDI-TOF mass spectrometry, amide proton hydrogen/deuterium exchange, chemical modifications

Selected Publications:

1. M.C. Maurer, C.C. Lester, E.E. DiBella, H.A. Scheraga (1999) “A New General Approach for Determining the Solution Structure of a Ligand Bound Weakly to a Receptor:  Structure of a Fibrinogen A-like Peptide Bound to Thrombin(S195A) Obtained Using NOE Distance Constraints and an ECEPP/3 Flexibile Docking Program” Proteins: Structure, Function, and Genetics, 34, 29-48.
2. T.A. Trumbo, M.C. Maurer (2000) “Examining Thrombin Hydrolysis of the Factor XIII Activation Peptide Segment Leads to a Proposal for Explaining the Cardioprotective Effects    Observed With the Factor XIII V34LMutation” J. Biol. Chem., 275, 20627-20631.
3. T.A. Trumbo, M.C. Maurer (2002) “Thrombin Hydrolysis of V29F and V34L Mutants of Factor XIII (28-41) Reveals Roles of the P9 and P4 Positions in Factor XIII Activation”     Biochemistry, 41, 2859-68.
4. B.T. Turner, M.C. Maurer (2002) “Evaluating the Roles of Thrombin and Calcium in Activation of Coagulation Factor XIII Using H/D Exchange and MALDI-TOF MS” Biochemistry 41, 7947 7954.
5. D.B. Cleary, T.A. Trumbo, M.C. Maurer (2002) “PAR4-like Peptides Bind to Thrombin Through an Optimized Interaction With the Enzyme Active Site Surface” Archives of Biochemistry and Biophysics 403, 179-188.
6. A. Marinescu, D.B. Cleary, T.R. Littlefield, M.C. Maurer (2002) “Exploring the Substrate  Specificity of Factor XIII for Glutamine-Containing Peptides Using Solution NMR Methods” Archives of Biochemistry and Biophysics 406, 9-20.
7. D.B. Cleary, W.D. Erhinger, M.C. Maurer (2003) “Establishing the Inhibitory Effects of Bradykinin on Thrombin” Archives of Biochemistry and. Biophysics. 410, 96-106.
8. T.A. Trumbo, M.C. Maurer (2003) “V34I and V34A Substitutions Within the Factor XIII Activation Peptide Segment (28-41) Affect Interactions With the Thrombin Active Site.” Thrombosis and Haemostasis. 89, 647-53.
9. G. Isetti, M.C. Maurer (2004) “Probing Thrombin's Ability to Accommodate a V34F Substitution Within the Factor XIII Activation Peptide Segment (28-41)” J. Peptide Research, 63, 241-252.
10. G. Isetti, M.C. Maurer (2004) “Thrombin Activity is Unaltered by N-terminal Truncation of Factor XIII Activation Peptides” Biochemistry 43, 4150-4159.
11. B.T. Turner Jr., T.M. Sabo, D. Wilding, M.C. Maurer (2004) “Mapping of Factor XIII Solvent Accessibility as a Function of Activation State Using Chemical Modification Methods” Biochemistry 43, 9755-65.
12. M.C. Maurer, T.A. Trumbo, G. Isetti, B.T. Turner Jr. (2006) “Probing Interactions Between the Coagulants Thrombin, Factor XIII, and Fibrin(ogen)” Archives of Biochemistry and Biophysics 445, 36-45.
13. T.M. Sabo, D.H. Farrell, M.C. Maurer (2006) “Conformational Analysis of γ′ Peptide (410-427) Interactions With Thrombin Anion Binding Exosite II” Biochemistry 45, 7434-45.
14. D.B. Cleary, M.C. Maurer (2006) “Characterizing the Specificity of Activated Factor XIII for Glutamine-Containing Substrate Peptides” Biochim. Biophys. Acta 1764, 1207-1217.
15. G. Isetti, M.C. Maurer (2007) “Employing Mutants to Study Thrombin Residues Responsible for Factor XIII Activation Peptide Recognition:  A Kinetic Study” Biochemistry 46, 2444-2452.
16. T.M. Sabo, P.B. Brasher, M.C. Maurer (2007) “Perturbations in Factor XIII Resulting From Activation and Inhibition Conditions Examined by Solution Based Methods and Detected by MALDI-TOF MS” Biochemistry 46, 10089-10101.