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    Perturbation of Triple-Helix Structure in Mutant Collagens Examined by Subnanosecond Local Dynamics of Tryptophan: An Application of Time-Resolved Fluorescence Anisotropy

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    Author
    Paul, R. Dawn
    Advisor
    Dawn Bregel; Ron Wilde; Joan Stottlemyer
    Date of Issue
    2005-04-01
    Metadata
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    URI
    https://scholars.carroll.edu/handle/20.500.12647/2940
    Title
    Perturbation of Triple-Helix Structure in Mutant Collagens Examined by Subnanosecond Local Dynamics of Tryptophan: An Application of Time-Resolved Fluorescence Anisotropy
    Type
    thesis
    Abstract
    Time-resolved fluorescence anisotropy can provide information about the local dynamic properties of a molecule at sub-nanometer resolution on the nano- and picosecond time scales. To help explain perturbations of the triple-helical structure of collagen induced by a mutation, and to facilitate an understanding of mutations associated with diseases like scurvy, an examination of synthetic collagen-like peptides was conducted. Results indicate that the extent of local motion increases near a mutation, demonstrating that the change in the amino acid interrupts the helical structure. Local motion, however, remains unchanged several amino acid residues away from the indole side chain of the tryptophan residue. In addition, the perturbation of the helical structure is asymmetric as there is an increase in the local motion of the indole side chain farther to the C-terminal side of the mutation.
    Degree Awarded
    Bachelor's
    Semester
    Spring
    Department
    Life & Environmental Sciences
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    • Life and Environmental Sciences Undergraduate Theses

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