Major
Chemistry
Anticipated Graduation Year
2020
Access Type
Open Access
Abstract
Proteins are the molecules that make life possible. Protein sequences are random, by and large. This makes it challenging to infer component identity and functions, given partial information about a sequence. In this research, we observe a conservation principle of functional uncertainty at the amino acid sites. Significantly, functional uncertainty was found to be a conserved property across archetypal proteins and proteomes. Further, the information of at least 1000 proteins is required for uncertainty for maximum correlations and conservation. Just as important, we show how viral systems diverge from living in that they are not subject to functional uncertainty conservation.
Faculty Mentors & Instructors
Dr. Daniel Graham, Professor, Department of Chemistry and Biochemistry
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
The Conservation of Functional Uncertainty in Biological Proteins
Proteins are the molecules that make life possible. Protein sequences are random, by and large. This makes it challenging to infer component identity and functions, given partial information about a sequence. In this research, we observe a conservation principle of functional uncertainty at the amino acid sites. Significantly, functional uncertainty was found to be a conserved property across archetypal proteins and proteomes. Further, the information of at least 1000 proteins is required for uncertainty for maximum correlations and conservation. Just as important, we show how viral systems diverge from living in that they are not subject to functional uncertainty conservation.