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Full-Text Articles in Physical Sciences and Mathematics
Environments Of The Four Tryptophans In The Extracellular Domain Of Human Tissue Factor: Comparison Of Results From Absorption And Fluorescence Difference Spectra Of Tryptophan Replacement Mutants With The Crystal Structure Of The Wild-Type Protein, C. A. Hasselbacher, E. Rusinova, R. Rusinova, R. A. Kohanski, W. Lam, A. Guha, J. Du, T. C. Lin, I. Polikarpov, C. W. G. Boys, Y. Nemerson, W. H. Konigsberg, J. B. A. Ross
Environments Of The Four Tryptophans In The Extracellular Domain Of Human Tissue Factor: Comparison Of Results From Absorption And Fluorescence Difference Spectra Of Tryptophan Replacement Mutants With The Crystal Structure Of The Wild-Type Protein, C. A. Hasselbacher, E. Rusinova, R. Rusinova, R. A. Kohanski, W. Lam, A. Guha, J. Du, T. C. Lin, I. Polikarpov, C. W. G. Boys, Y. Nemerson, W. H. Konigsberg, J. B. A. Ross
Chemistry and Biochemistry Faculty Publications
The local environments of the four tryptophan residues of the extracellular domain of human tissue factor (sTF) were assessed from difference absorption and fluorescence spectra. The difference spectra were derived by subtracting spectra from single Trp-to-Phe or Trp-to-Tyr replacement mutants from the corresponding spectrum of the wild-type protein. Each of the mutants was capable of enhancing the proteolytic activity of factor Vila showing that the mutations did not introduce major structural changes, although the mutants were more susceptible to denaturation by guanidinium chloride. The difference spectra indicate that the Trp residues are buried to different extents within the protein matrix. …