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Study of Physical Protein-Protein Interactions Between the MaSp1 C-Terminal Domain and Small Cysteine-Rich Proteins Found in the Major Ampullate Gland of Latrodectus hesperus

Author

Taylor Renee Rabara, University of the PacificFollow

Date of Award

2016

Document Type

Thesis - Pacific Access Restricted

Degree Name

Master of Science (M.S.)

Department

Biological Sciences

First Advisor

Craig A. Vierra

First Committee Member

Geoffrey Lin-Cereghino

Second Committee Member

Lisa A. Wrishnick

Abstract

Spiders spin a wide variety of different silk types with different biological functions that are known for their extraordinary mechanical properties. Dragline silk has predominantly captured the interest of researchers because it exhibits high tensile strength and toughness while maintaining its elasticity. This thesis has focused on the characterization of a family of small molecular weight proteins recently discovered in dragline silk. These proteins were discovered in the western black widow spider, Latrodectus hesperus, and have been termed Cysteine-Rich Proteins (CRPs) due to their high conserved cysteine content. CRP family members were used in protein-protein interaction studies to determine if there is any interaction with the major ampullate spidroins (MaSps). After affinity chromatography and co-expression studies in bacteria, there were no detectable interactions between the CRPs and MaSp1. Further studies

which could be an important role in the natural silk assembly process. Further protein interaction studies in different salt and pH conditions can further determine the function of the CRPs in dragline silk formation.

Recommended Citation

Rabara, Taylor Renee. (2016). Study of Physical Protein-Protein Interactions Between the MaSp1 C-Terminal Domain and Small Cysteine-Rich Proteins Found in the Major Ampullate Gland of Latrodectus hesperus. University of the Pacific, Thesis - Pacific Access Restricted. https://scholarlycommons.pacific.edu/uop_etds/2965