Research in the Maurer Group focuses on protein chemistry and protein structure-function relationships. We are particularly interested in enzymes involved in blood coagulation and related processes. Members of this critical protein cascade have far reaching effects on wound healing, heart disease, stroke, and cancer. Further knowledge is still needed on the activation, regulation, and substrate/ligand binding properties of individual players. In our laboratory, emphasis is placed on examining the transglutaminase Factor XIII (FXIII), the serine protease thrombin, and the structural protein fibrinogen. These proteins work together to create a strong, covalently linked blood clot network. For our research studies, we employ a variety of biochemical, bioanalytical, and biophysical methods including protein expression/purification, enzymatic kinetic studies (uv-vis and HPLC based), solution NMR, mass spectrometry, and analytical ultracentrifugation approaches. Greater understanding of the biochemical and biophysical features of FXIII, thrombin, and fibrinogen may lead to novel medical strategies to control the actions of these vital proteins and the resultant blood clot architecture.