Research
Protein Kinetic Stability
While most proteins transiently unfold and turnover, Kinetically Stable Proteins (KSPs) are trapped by elevated free energy barriers causing them to maintain their structures for prolonged periods of time. This hyperstability causes KSPs to show resistances to proteases and denaturants including the detergent SDS. The Colón lab exploits this SDS-resistance through the Diagonal Two-Dimensional Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis (D2D SDS-PAGE) method which allows KSPs to be isolated from complex lysates and protein mixtures. Once KSPs are isolated on a gel, they can be identified through peptide mass fingerprinting. While KSPs have been found in nearly every sample tested, certain organisms appear to possess functional trends in their KSPs that exhibits implications towards various applications.
Extremophilic Microorganisms contain an abundance of KSPs when compared to their mesophilic counterparts. This increased protein stability likely developed to allow extremophiles to thrive in environments typically considered stressful including high temperature, low pH, and high pressure. Identifying hyperstable proteins from these organisms may pave the way for commercial and industrial biotechnology applications. Possibly the most notable application of an extremophilic KSP would be the revolution of molecular biology by Taq polymerase (derived from the thermophile Thermus aquaticus) for PCR.
Human Plasma displays a diverse set of KSPs when subjected to the D2D SDS-PAGE method. Interestingly, there appear to be slight differences in the KSP expression profile depending on the patient tested. Testing for the presence and abundance of these KSPs may act as a biomarker assay for disease detection as many illnesses are linked to the presence or aggregation of hyperstable proteins.
Plants and Seeds contain highly-abundant storage proteins, such as phaseolin and 8Sα globulin, which have been shown to possess kinetic stability. These proteins may allow seeds and legumes to both hold their long shelf-lives as well as promote dietary intolerances associated with their consumption. It may be possible to manipulate this native hyperstability to confer agricultural prosperity, perhaps through increased pest-resistance.
Over 300 hyperstable proteins are currently known, both from identification in the Colón Lab and from current literature. Outside of the simple identification of hyperstable proteins, bioinformatic analysis of KSPs can lead to elucidation of structural and functional trends common to hyperstable proteins. This information could lead to the design of proteins with increased stability for biotechnological application which may have a wide range of uses benefiting society.
Extremophilic Microorganisms contain an abundance of KSPs when compared to their mesophilic counterparts. This increased protein stability likely developed to allow extremophiles to thrive in environments typically considered stressful including high temperature, low pH, and high pressure. Identifying hyperstable proteins from these organisms may pave the way for commercial and industrial biotechnology applications. Possibly the most notable application of an extremophilic KSP would be the revolution of molecular biology by Taq polymerase (derived from the thermophile Thermus aquaticus) for PCR.
Human Plasma displays a diverse set of KSPs when subjected to the D2D SDS-PAGE method. Interestingly, there appear to be slight differences in the KSP expression profile depending on the patient tested. Testing for the presence and abundance of these KSPs may act as a biomarker assay for disease detection as many illnesses are linked to the presence or aggregation of hyperstable proteins.
Plants and Seeds contain highly-abundant storage proteins, such as phaseolin and 8Sα globulin, which have been shown to possess kinetic stability. These proteins may allow seeds and legumes to both hold their long shelf-lives as well as promote dietary intolerances associated with their consumption. It may be possible to manipulate this native hyperstability to confer agricultural prosperity, perhaps through increased pest-resistance.
Over 300 hyperstable proteins are currently known, both from identification in the Colón Lab and from current literature. Outside of the simple identification of hyperstable proteins, bioinformatic analysis of KSPs can lead to elucidation of structural and functional trends common to hyperstable proteins. This information could lead to the design of proteins with increased stability for biotechnological application which may have a wide range of uses benefiting society.