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Bioinformatics
Protein Cloning Expression
X-ray Crystalography
Protein Crystallization
Our primary goal is to investigate how the diversity and abundance of life are reflected upon the molecular stability and specificity of proteins that are determined by its three-dimensional (3D) structures.
There is a long and rich history in the use of primary sequence information of proteins to detect homology, to build phylogenetic trees, and to establish evolutionary relationships. Today, the availability of vast databases of gene sequences and amino sequences make sequence-aligning approaches a powerful and widely used tool. However, there are inherent limitations to this approach. The function of a protein depends upon its three-dimensional structure not its primary sequence. It is now well established that proteins can be topologically and functionally equivalent even when there is no detectable sequence homology. Even more perplexing, proteins with similar sequences can have different folds and different functions. Unfortunately, structures are available for only a small fraction of the proteins for which sequences are known; more three-dimensional information is needed. We need to understand better the structural principles that governed the evolution of proteins and the mechanisms used to acquire new or modified functions. To better understand the structural principles that govern the evolution of proteins, their structure and their function, it is necessary to comprehend how they are adapted to function in the extreme range of environments in which life is found. Thus we address the questions by studying evolution and the limits to life as revealed in the related three-dimensional molecular structures of proteins from extreme thermophilic microbes (hyperthermophiles) using X-ray crystallography, and compare their structures with those from organisms found in the three domains of life.
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