University of California, Irvine, Department of Biological Sciences, Molecular Biology and Biochemistry

Dr. Agnes Henschen-Edman

(M.D./Ph.D., Karolinska Institute (Stockholm), 1964)

Protein structure, function, post-translational modification; fibrinogen

  • Faculty Profile

    Publications via PubMed (NIH National Library of Medicine)

  • E-mail: ahensche@uci.edu


  • The elucidation of the covalent structure of a protein is a prerequisite for the understanding of its biological function. In our group, the primary structures, post-translational modifications, and structure-function relationships of several biologically and medically important proteins are being studied. Fibrinogen is a central protein of blood coagulation and has a molecular weight of about 340 kDa. The proteolytic enzyme thrombin converts it into an insoluble form, the fibrin clot. The diseases related to the blood coagulation system are of great medical interest, and therefore it is important to understand the structure-function relationships in fibrinogen. Genetically determined, dysfunctional variants of fibrinogen can be used as highly specific probes for these relationships, as each mutation which causes an amino acid substitution may provide clues about a functional site. So far, the variants from over 60 families have been structurally elucidated, many of them by our research group. However, in every person fibrinogen is also extensively post-translationally modified , and the identification and functional properties of the corresponding variants are also being studied in the laboratory. The investigations are relevant for the understanding of the role of fibrinogen in thrombotic cardiovascular disease and bleeding disorders. Furthermore, fibrinogen is well-suited as a model for studying structure-function relationships in a multi-functional protein, as it interacts in a highly specific way with a number of proteins, with cell surface receptors, and with certain ions.
    Dr. Henschen-Edman is part of the UCI Graduate Track in Structural Biology and Molecular Biophysics within the UCI graduate Program in Molecular Biology, Genetics, and Biochemistry. Applications requests or additional information about the graduate program may be obtained by electronic mail at gp-mbgb@uci.edu or by phone at (949) 824-8145. On-line applications may also be submitted through the Office of Research and Graduate Studies.

    1) Molecular Biology, Genetics, and Biochemistry

    2) Email: gp-mbgb@uci.edu or call (949) 824-8145

    3) Graduate Studies Home Page, with links to On-line applications and the Office of Research and Graduate Studies


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