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Journal of Undergraduate Research

Keywords

genetic analysis, protein folding, SbtE, ISP

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

Proteins are of the utmost physiological importance in their roles as enzymes, structural elements, and antibodies. Correctly formed proteins catalyze biochemical reactions, initiate proper immune system response, and even promote the development of hair, bones, skin, muscles, and blood. Likewise, incorrectly formed proteins cause Alzheimer’s disease, cystic fibrosis, various forms of cancer, and Creutzfeld-Jacob (mad cow) disease1. One of the fundamental problems that scientists face today is understanding how proteins fold to yield correct or incorrect structures. Proteins consist of building blocks called amino acids, each of which is encoded by certain DNA sequences. The conventional wisdom in the field is that small DNA sequence changes make little difference in the folding pathway of a protein. However, recent studies by Subbian et al. suggest that these small differences may have powerful effects.

Included in

Chemistry Commons

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