ABSTRACT
Physical remains of ancestor nucleotides and proteins are largely unavailable; thus, sequence comparison between homologous genes in present-day organisms forms the basis for the current knowledge of molecular evolution. However, variation in protein three-dimensional structure is the foundation for functional diversity and pathological mutations. To understand the evolutionary relationship of three-dimensional structures in related proteins would have major impacts on our understanding of the diversity as well as conservation of biological processes. A protein may contain ancestor conformations that have been allosterically suppressed or modiied by evolutionarily added structures. Using polyclonal and monoclonal antibodies as three-dimensional nanostructure
probes to detect such conformation in proteins after removing the suppressor/modiier structure, we have demonstrated the feasibility to detect evolutionarily suppressed ancestor-like conformational states in proteins. In addition to identifying structural modiications that were critical to the emerging of diverged proteins, investigating protein evolution using this novel approach will help to understand the origin as well as functional potential of existing protein structures.
