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Thermal stability of refractory and ceramic materials in atomic reactors, rockets, and jet engines
Traditional methods for fabricating nanoscale arrays are usually based on lithographic techniques. Alternative new approaches rely on the use of nanoscale templates made of synthetic or biological materials. Some proteins, for example, have been used to form ordered two-dimensional arrays. Here, we fabricated nanoscale ordered arrays of metal and semiconductor quantum dots by binding preformed nanoparticles onto crystalline protein templates made from genetically engineered hollow double-ring structures called chaperonins. Using structural information as a guide, a thermostable recombinant chaperonin subunit was modified to assemble into chaperonins with either 3 nm or 9 nm apical pores surrounded by chemically reactive thiols. These engineered chaperonins were crystallized into two-dimensional templates up to 20 microm in diameter. The periodic solvent-exposed thiols within these crystalline templates were used to size-selectively bind and organize either gold (1.4, 5 or 10nm) or CdSe-ZnS semiconductor (4.5 nm) quantum dots into arrays. The order within the arrays was defined by the lattice of the underlying protein crystal. By combining the self-assembling properties of chaperonins with mutations guided by structural modelling, we demonstrate that quantum dots can be manipulated using modified chaperonins and organized into arrays for use in next-generation electronic and photonic devices.
Carbon capture and storage has been a research area of great interest in recent years asa method for mitigation of CO2emissions, due to the effects of climate change. The development of technologies for the efficient capture of CO2are also of great interest for human spaceflight applications. One of the most promising technologies in this area is CO2 scrubbing using liquid amines, unfortunately, liquid amines with low heats of desorption tend to have slow CO2binding kinetics. One potential solution to this problem is to use the enzyme carbonic anhydrase (CA) to enhance the kinetics of CO2binding to liquid amines, allowing the overall process to be more energy efficient. Interest in using carbonic anhydrase as a biocatalyst has led to a number of efforts to improve the thermostability and solvent tolerance of several distinct carbonic anhydrase enzymes. In the work described here, we screened through a diverse set of natural carbonic anhydrases to identify candidates for protein engineering aimed at increased stability and activity in various liquid amines. We then used SCHEMA structure-guided recombination to develop a set of chimeric carbonic anhydrases with high thermostability and activity. These chimeras were used as the starting points for further protein engineering work targeting activity in liquid amine systems. Our ultimate goal is to test the engineered enzymes in a liquid amine system for cabin air revitalization on ISS or other spacecraft.
Carbon capture and storage has been a research area of great interest in recent years as a method for mitigation of CO2 emissions, due to the effects of climate change. The development of technologies for the efficient capture of CO2 are also of great interest for human spaceflight applications. One of the most promising technologies in this area is CO2 scrubbing using liquid amines, unfortunately, liquid amines with low heats of desorption tend to have slow CO2 binding kinetics. One potential solution to this problem is to use the enzyme carbonic anhydrase (CA) to enhance the kinetics of CO2 binding to liquid amines, allowing the overall process to be more energy efficient. Interest in using carbonic anhydrase as a biocatalyst has led to a number of efforts to improve the thermostability and solvent tolerance of several distinct carbonic anhydrase enzymes. In the work described here, we screened through a diverse set of natural carbonic anhydrases to identify candidates for protein engineering aimed at increased stability and activity in various liquid amines. We then used SCHEMA structure-guided recombination to develop a set of chimeric carbonic anhydrases with high thermostability and activity. These chimeras were used as the starting points for further protein engineering work targeting activity in liquid amine systems. Our ultimate goal is to test the engineered enzymes in a liquid amine system for cabin air revitalization on ISS or other spacecraft.