Abstract
How does a protein's energy landscape change over an evolutionary time scale, and could a study of ancestral sequences reveal novel features of the landscape? Although there has been significant advances protein structure prediction from its primary sequence, extracting features of the entire energy landscape remains a challenge. There is limited understanding on how variations in the sequence that take place over the course of an evolutionary time scale change the landscape to yield novel properties and function. Past research on the landscape has focused on extant proteins, which represent only a small portion of proteins that have existed since the origin of life. Examining the ancestors of current proteins should provide additional insight into the properties of proteins and the process of protein evolution, and ultimately, further our understanding of the depth of information encoded within an amino acid sequence. We conducted an ancestral sequence reconstruction of ribonuclease H1, a biophysically well-characterized protein. A total of seven ancestral proteins along the mesophilic and thermophilic lineages were constructed and studied. This study reports on the characterization of the folding pathway and stability of the last common ancestral protein between E. coli and T. thermophilus ribonucleases H.
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