phone: (787) 832-4040 ext. 2302 email: belinda.pastrana@upr.edu office: Q-372G website: http://academic.uprm.edu/pastranaslab Lab: Q-385/307 Group Members:

EducationPh.D. Rutgers University, 1995Post-Doc Pharmacology, Biochemistry & Molecular Biology, Mayo Clinic & Foundation, Rochester, MN, 1995Recognitions2015 PHI KAPPA PHI Honor Society 2013 Honorary Member of the Golden Key International Honour Society University of Puerto Rico Mayaguez Campus 2011 ACS UPRM Student Chapter Distinguished Women Chemist 2011 International Year of Chemistry (IYC) Award to Distinguished Women in Chemistry and Chemical Engineering in Puerto Rico 2009 Henry Dreyfus Teacher Scholar Award, University of Puerto Rico, Mayagüez CampusTeaching InterestsGeneral Biochemistry I. CHEM5071 This is a three credit course, with three lecture hours per week. Chemical characterization of proteins, lipids, carbohydrates, and nucleic acids; principles of enzymology and bioenergetics, recombinant DNA techniques, introduction to carbohydrate metabolism and biological oxidations.General Biochemistry Laboratory II. CHEM5074 One credit hour. Four hours laboratory per week. Co-requisite: CHEM5071 The use of bioinformatics, structural genomics, and the molecular modeling in the spectroscopic characterization and analysis of biological molecules. Undergraduate Research I. CHEM4998 One to three credit hours. Three to nine hours of research per week. Pre-requisite: Authorization of the Director of the Department. Introduction to chemical research under the supervision of professors of the Chemistry department.Undergraduate Research II. CHEM4999 One to three credit hours. Three to nine hours of research per week. Pre-requisite: three credits in CHEM4998. A research project under the supervision of professors of the Chemistry department. Advanced undergraduate and graduate.Advanced Biochemistry. CHEM6715 Three credits, three hours of lectures per week. Study of the structure and function of biological macromolecules, such as nucleic acids and proteins. Discussion of biological membranes as fundamental components in cellular function. Analysis of macromolecules by advanced instrumental techniques.Biophysical Chemistry. CHEM6016 Three credit conference hours. Pre-requisite:CHEM6715 Spectroscopic methods, molecular simulation, bioenergetics, reaction kinetics, and solution thermodynamics applied to nucleic acids, proteins, and other biological molecules.Bioinformatics, Proteins, and Protein-Protein Interactions. CHEM8995 Four credits, four hours of lectures per week. Pre-requisite: CHEM6715 Bioinformatics its basic concepts, methods, and tools to assess protein sequence structure and function; and the use of molecular biophysics to study proteins and protein-protein interactions. Specifically, the students will have a hands-on approach to using bioinformatics databases to analyze sequences, phylogeny, protein homology, identifying common protein motifs and domains, and protein-protein interactions. Advanced analysis of thermodynamic and spectroscopic data will be performed to understand protein unfolding, relative stability, and protein-protein interactions. Molecular modeling will also be used to discuss protein structure and protein complexes.Graduate Co-op Project. CHEM6994 Credits: 3 credit hours, may be repeated once. New Special Topics course allowing graduate students have a work experience in the industry. The student must be in good standing, have a letter offer describing his/her responsibilities, tasks, period of work, immediate supervisor, division, company address and contact information. A Co-op collaboration agreement. Supervisor and advisor evaluations, mid-term report and final oral presentation are required. Guidelines for mid-term report and oral presentation, course syllabus, evaluation forms and collaboration agreement are included.Chemistry Research I, II, S. CHEM6998 Six credit hours. The student will choose a member of the faculty as his adviser. Presentation of a thesis is required for credit.Research InterestsUnderstanding protein interactions and their function by the use of molecular biophysical techniques. Selected Publications Pastrana-Rios, B., Sosa, L. D.V., and Santiago J., “TFA as excipient destabilizes melittin causing the selective aggregation of melittin within the Centrin-Melittin-TFA Complex” 2015 (In Press Structural Dynamics).  Pastrana-Rios, B. “Thermal Perturbation Correlation of a Calcium binding Human centrin 3 and its structural changes” 2014 J. Molecular Structure 1069(8), 85-88.  Ocaña, W., and Pastrana-Rios, B. “Calcium titration of Chlamydomonas centrin and its structural changes” 2014 J. Molecular Structure 1069(8), 73-78.  Narváez-Pita X., Ortega-Zuniga, C., Acevedo-Morantes, C.Y., Pastrana, B. Olivero-Verbel, J., Maldonado, W., and Meléndez E. “Water soluble molybdenocene complexes: Synthesis, cytotoxic activity and binding studies to ubiquitin by fluorescence spectroscopy, circular dichroism and molecular modeling” 2013 J. Inorganic Biochemistry 132, 77-91. PMID: 24287102.  Pastrana-Rios, B., Reyes, M. Meza, V., De Orbeta, J. Rodriguez Nassif, A., Narváez, D., Gómez, A.M., Almodovar, R., Díaz, A., Robles, J., Irizarry, L., Campbell, M., and Colón, M. 2013 “Relative stability of Centrins and its Relationship with Calcium Binding” Biochemistry 52, 1236-1248. PMID: 23346931.  Sosa, L. D.V., Alfaro, E., Santiago, J., Narváez, D., Rosado, M.C., Rodríguez, A., Gómez, A.M., Schreiter, E., and Pastrana-Rios, B. “The Structure, Molecular Dynamics, and Energetics of Centrin-Melittin Complex” 2011 Proteins: Structure, Function, and Bioinformatics 79, 3132-3143. PMID: 21989934.