2026-09-18T20:17:05Zhttps://ecommons.cornell.edu/server/oai/requestoai:ecommons.cornell.edu:1813/1992026-07-07T15:02:19Zcom_1813_35col_1813_47
Lautenschlager, Catherine
2004-11-10T14:52:10Z
2004-11-10T14:52:10Z
2004-11-10T14:52:10Z
https://hdl.handle.net/1813/199
6475957
Jon Clardy, Steve Ealick, Jerrold Meinwald, Brian Crane
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.
NIH
9116658 bytes
application/pdf
en_US
pheromone binding protein
pantocin A
Bombyx mori
x-ray crystallography
Structural Studies of Protein-Small Molecule Interactions: Bombyx Mori Pheromone Binding Protein Specificity for Bombykol, and the Substrate Specificity of Pantocin A Biosynthetic Proteins
dissertation or thesis
application/pdf
Publication
Cornell Theses and Dissertations
Lautenschlager, Catherine
5893a6ea-7af3-41d7-abc6-04bcd26ab5df
COMPLETE
open.access
open.access
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<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</Title>
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<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.</Abstract>
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