Skip to main content


eCommons@Cornell

eCommons@Cornell >
Cornell University Graduate School >
Theses and Dissertations (OPEN) >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1813/199
Title: Structural Studies of Protein-Small Molecule Interactions: Bombyx Mori Pheromone Binding Protein Specificity for Bombykol, and the Substrate Specificity of Pantocin A Biosynthetic Proteins
Authors: Lautenschlager, Catherine
Keywords: pheromone binding protein
pantocin A
Bombyx mori
x-ray crystallography
Issue Date: 10-Nov-2004
Abstract: Interactions between small molecules and proteins mediate the biological processes of life. A knowledge of how proteins specifically interact with small molecules provides us with the tools to probe complex biology, but also allows us to develop potent and specific drugs to manipulate these processes to prevent, manage and cure disease. In the first part of this thesis, the interactions between non-pheromone small molecules and the pheromone binding protein from Bombyx mori were explored by using X-ray crystallography to solve structures of these complexes. Pheromone signal transduction in moths provides a relatively simple model of the complex biology of neurological processing. The second part of this thesis aimed to discover the functional form of a peptide substrate that interacts with biosynthetic enzymes to make pantocin A. This antibiotic is effective against Erwinia amylovora, the pathogen that causes fire blight disease. The functional form of the substrate was explored through genetic manipulation of the biosynthetic pathway that produces pantocin A.
Description: Jon Clardy, Steve Ealick, Jerrold Meinwald, Brian Crane
URI: http://hdl.handle.net/1813/199
Appears in Collections:Theses and Dissertations (OPEN)

Files in This Item:

File Description SizeFormat
catthesis.pdf8.9 MBAdobe PDFView/Open

Refworks Export

Items in eCommons are protected by copyright, with all rights reserved, unless otherwise indicated.

 

© 2014 Cornell University Library Contact Us