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Organic Chemistry

University of Arkansas, Fayetteville

2004

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The Effects Of Multiple Mutations In The Hydrophobic Core Upon The Stability Of Staphylococcal Nuclease, Rebecca L. Danforth Jan 2004

The Effects Of Multiple Mutations In The Hydrophobic Core Upon The Stability Of Staphylococcal Nuclease, Rebecca L. Danforth

Inquiry: The University of Arkansas Undergraduate Research Journal

Previous work in the laboratory of my research advisor, Dr. Wesley Stites, has investigated the core packing of the protein staphylococcal nuclease. The core of a protein is critical in determining a protein's structure and stability. The hydrophobicity of the core has long been thought to be the principal driving force for folding, but recent work in the Stites lab has shown that optimization of van der Waals contacts and minimization of cavities, in our shorthand term, packing, is at least as energetically important. We are building upon this information in our attempt to better pack the protein core. If …