Title

Unraveling the Mysteries of Di-tyrosine Linkages in Spider Silk Using the Mass Spectrometer

Poster Number

15

Format

Poster Presentation

Abstract/Artist Statement

Spider silks are known to have intriguing physical properties such as being lightweight extremely strong and elastic, which would be very valuable to the commercial industry. If the genes could be isolated and synthetically manufactured the possibilities are numerous, ranging from bullet- proof vests to stronger building materials. However, the formation of this silk is a mystery that is still being unraveled. The hypothesis was that two tyrosine amino acids may be able to link up with either each other or with other proteins to precipitate a solid from the liquid inside the glands. These peptide chains may either link to each other (3B1-3B1) or to the other peptide (3B1-MaSp2). Our research has gone into investigating the possibilities of how the mechanism of silk formation in the black widow spider, Latrodectus Hesperus. The primary focus of our work has gone into exploring the existence of di-tyrosine cross link formations, particularly by that of the protein 3B1. Under varying pH and temperature environments, it was attempted to determine under what conditions the linkages formed. Taking whole cell extracts and individual glands, the mass spectrometer was used to help identify any changes in protein weight that could represent the formation of any di-tyrosine cross-linkage.

Location

Pacific Geosciences Center

Start Date

5-5-2007 1:00 PM

End Date

5-5-2007 3:00 PM

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May 5th, 1:00 PM May 5th, 3:00 PM

Unraveling the Mysteries of Di-tyrosine Linkages in Spider Silk Using the Mass Spectrometer

Pacific Geosciences Center

Spider silks are known to have intriguing physical properties such as being lightweight extremely strong and elastic, which would be very valuable to the commercial industry. If the genes could be isolated and synthetically manufactured the possibilities are numerous, ranging from bullet- proof vests to stronger building materials. However, the formation of this silk is a mystery that is still being unraveled. The hypothesis was that two tyrosine amino acids may be able to link up with either each other or with other proteins to precipitate a solid from the liquid inside the glands. These peptide chains may either link to each other (3B1-3B1) or to the other peptide (3B1-MaSp2). Our research has gone into investigating the possibilities of how the mechanism of silk formation in the black widow spider, Latrodectus Hesperus. The primary focus of our work has gone into exploring the existence of di-tyrosine cross link formations, particularly by that of the protein 3B1. Under varying pH and temperature environments, it was attempted to determine under what conditions the linkages formed. Taking whole cell extracts and individual glands, the mass spectrometer was used to help identify any changes in protein weight that could represent the formation of any di-tyrosine cross-linkage.