Abstract
Understanding the structural and dynamic information encoded in the primary sequence of a protein is one of the most fundamental challenges in modern biology. Most studies of protein design and ligand binding are extremely native-state centric, ignoring the role of a protein's energy landscape. The amino acid sequence of a protein, however, encodes more than the native three-dimensional structure; it encodes the entire energy landscape - an ensemble of conformations whose energetics and dynamics are finely tuned for folding, binding and activity. I will present our results demonstrating that for proteins without a well-folded native state, small sequence variation can have dramatic effects on ligand binding and specificity. I will also present single-molecule studies demonstrating that small changes in the sequence and environment can alter the folding trajectory of a protein.
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