Understanding the structural and dynamic information encoded in the primary sequence of a protein is one of the most fundamental challenges in modern biology. The amino acid sequence of a protein 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. Small variations in the sequence and environment modulate this landscape and can have effects that range from undetectable to pathological. I will present our recent experimental results probing these sequence and environmental effects on the landscape following different reaction coordinates, using a combination of single-molecule and ensemble-based studies. The quantitative nature of our studies, provides a unique platform to test simulation methods, which should enhance the ability to connect experiments and theory.

Touring the landscape: The view depends on how you look

251st National Meeting (2016)

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